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Conserved domains on  [gi|2502538741|ref|WP_281869186|]
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AraC family transcriptional regulator [Brevibacillus parabrevis]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 11454428)

AraC family transcriptional regulator containing an AraC family helix-turn-helix (HTH) DNA-binding domain and a TroA-like periplasmic binding domain, similar to Bacillus subtilis HTH-type transcriptional activator Btr that activates expression of the feuABCybbA operon, which encodes the bacillibactin uptake system, in iron-limited conditions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TroA-like super family cl00262
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 383-629 9.16e-55

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


The actual alignment was detected with superfamily member cd01138:

Pssm-ID: 469696 [Multi-domain]  Cd Length: 248  Bit Score: 187.16  E-value: 9.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 383 GDVEIPVNPQRVVVFYLLGDVLALN-VKPVGISDVQKG--AAFEKELEGVQTLGTwfEPNPEAVLALDPDLIIAPS--EK 457
Cdd:cd01138     1 GEVEIPAKPKRIVALSGETEGLALLgIKPVGAASIGGKnpYYKKKTLAKVVGIVD--EPNLEKVLELKPDLIIVSSkqEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 458 IYQMMEKVAPTVYIPFDRMTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGILDKTVSIMEGGKGNMsvVS 537
Cdd:cd01138    79 NYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIY--VF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 538 SKDYGRGSQIVYEYLGMKAPAIVQAKLDKPsgeaTAESVSFEVLPQYAGDFVFRSAY---EGMVDLSDNKVWNSIPAIKE 614
Cdd:cd01138   157 GEDGRGGGPILYADLGLKAPEKVKEIEDKP----GYAAISLEVLPEFDADYIFLLFFtgpEAKADFESLPIWKNLPAVKN 232

                         250
                  ....*....|....*
gi 2502538741 615 GRLIEIDFGLSYYND 629
Cdd:cd01138   233 NHVYIVDAWVFYFAD 247
GlxA super family cl34854
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 177-279 3.82e-31

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


The actual alignment was detected with superfamily member COG4977:

Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 123.73  E-value: 3.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 177 AQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYY 256
Cdd:COG4977   213 ARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292

                          90       100
                  ....*....|....*....|...
gi 2502538741 257 FAKMFKRYTGASPIRYRTEQARR 279
Cdd:COG4977   293 FRRAFRRRFGVSPSAYRRRFRAR 315
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
22-279 1.65e-29

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 117.57  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741  22 YLALFREEASRAWQLPASSFLFATKGRAEIWLDGQKHPAQRFYMLHGGKGARLQICPLEDVFEYYVIYYKALLPLPMNQE 101
Cdd:COG2207     1 LRLLILLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 102 LIAMLERQRPFDAAYGFLPEKAVCLLQNIQLMHEEWEKRNGLEHFHVRALFYQVVYELLRQMHNPSLSRKPNDLAAQALG 181
Cdd:COG2207    81 LLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 182 YIQENYAQpLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMF 261
Cdd:COG2207   161 LLLLLLLL-LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAF 239

                         250
                  ....*....|....*...
gi 2502538741 262 KRYTGASPIRYRTEQARR 279
Cdd:COG2207   240 KKRFGVTPSEYRKRLRAR 257
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 383-629 9.16e-55

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 187.16  E-value: 9.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 383 GDVEIPVNPQRVVVFYLLGDVLALN-VKPVGISDVQKG--AAFEKELEGVQTLGTwfEPNPEAVLALDPDLIIAPS--EK 457
Cdd:cd01138     1 GEVEIPAKPKRIVALSGETEGLALLgIKPVGAASIGGKnpYYKKKTLAKVVGIVD--EPNLEKVLELKPDLIIVSSkqEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 458 IYQMMEKVAPTVYIPFDRMTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGILDKTVSIMEGGKGNMsvVS 537
Cdd:cd01138    79 NYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIY--VF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 538 SKDYGRGSQIVYEYLGMKAPAIVQAKLDKPsgeaTAESVSFEVLPQYAGDFVFRSAY---EGMVDLSDNKVWNSIPAIKE 614
Cdd:cd01138   157 GEDGRGGGPILYADLGLKAPEKVKEIEDKP----GYAAISLEVLPEFDADYIFLLFFtgpEAKADFESLPIWKNLPAVKN 232

                         250
                  ....*....|....*
gi 2502538741 615 GRLIEIDFGLSYYND 629
Cdd:cd01138   233 NHVYIVDAWVFYFAD 247
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 321-621 1.66e-46

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 167.02  E-value: 1.66e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 321 KSSLATILFLCLTLILGACSAPTTTSTANPGAEQPQVnsaasastsnqpsakpatkiVSTAKGDVEIPVNPQRVVV--FY 398
Cdd:COG4594     2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGART--------------------VKHAMGETTIPGTPKRVVVleWS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 399 LLGDVLALNVKPVGISDVQKG----AAFEKELEGVQTLGTWFEPNPEAVLALDPDLIIAPS---EKIYQMMEKVAPTV-- 469
Cdd:COG4594    62 FADALLALGVTPVGIADDNDYdrwvPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKsrhEAIYDQLSKIAPTVlf 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 470 -YIPFDRMTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGiLDKTVSIMEGGKGNMSVVSSKDYgRGSqiV 548
Cdd:COG4594   142 kSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAAD-KGKKVAVGQFRADGLRLYTPNSF-AGS--V 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2502538741 549 YEYLGMKAPaivqAKLDKPSGEATAEsVSFEVLPQYAGDFVFRSAYEGMV---DLSDNKVWNSIPAIKEGRLIEID 621
Cdd:COG4594   218 LAALGFENP----PKQSKDNGYGYSE-VSLEQLPALDPDVLFIATYDDPSilkEWKNNPLWKNLKAVKNGRVYEVD 288
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 177-279 3.82e-31

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 123.73  E-value: 3.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 177 AQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYY 256
Cdd:COG4977   213 ARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292

                          90       100
                  ....*....|....*....|...
gi 2502538741 257 FAKMFKRYTGASPIRYRTEQARR 279
Cdd:COG4977   293 FRRAFRRRFGVSPSAYRRRFRAR 315
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
22-279 1.65e-29

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 117.57  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741  22 YLALFREEASRAWQLPASSFLFATKGRAEIWLDGQKHPAQRFYMLHGGKGARLQICPLEDVFEYYVIYYKALLPLPMNQE 101
Cdd:COG2207     1 LRLLILLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 102 LIAMLERQRPFDAAYGFLPEKAVCLLQNIQLMHEEWEKRNGLEHFHVRALFYQVVYELLRQMHNPSLSRKPNDLAAQALG 181
Cdd:COG2207    81 LLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 182 YIQENYAQpLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMF 261
Cdd:COG2207   161 LLLLLLLL-LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAF 239

                         250
                  ....*....|....*...
gi 2502538741 262 KRYTGASPIRYRTEQARR 279
Cdd:COG2207   240 KKRFGVTPSEYRKRLRAR 257
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
190-273 3.81e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 107.64  E-value: 3.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741  190 PLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASP 269
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2502538741  270 IRYR 273
Cdd:smart00342  81 SEYR 84
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 370-621 3.68e-26

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 108.99  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 370 SAKPATkiVSTAKGDVEIPVNPQRVVVF-YLLGDVLA-LNVKPVGISDVQKG----AAFEKELEGVQTLGTWFEPNPEAV 443
Cdd:PRK11411   20 HAFAVT--VQDEQGTFTLEKTPQRIVVLeLSFVDALAaVGVSPVGVADDNDAkrilPEVRAHLKPWQSVGTRSQPSLEAI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 444 LALDPDLIIAPSEK---IYQMMEKVAPTVYIPFDRMTVEERLQ---KLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAg 517
Cdd:PRK11411   98 AALKPDLIIADSSRhagVYIALQKIAPTLLLKSRNETYQENLQsaaIIGEVLGKKREMQARIEQHKERMAQFASQLPKG- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 518 ildKTVSIMEGGKGNMSVVSSKDYGrGSqiVYEYLGMKAPAivqakldKPSGEATAESVSFEVLPQYAGDFVFRSAY--E 595
Cdd:PRK11411  177 ---TRVAFGTSREQQFNLHSPESYT-GS--VLAALGLNVPK-------APMNGAAMPSISLEQLLALNPDWLLVAHYrqE 243

                         250       260
                  ....*....|....*....|....*..
gi 2502538741 596 GMVD-LSDNKVWNSIPAIKEGRLIEID 621
Cdd:PRK11411  244 SIVKrWQQDPLWQMLTAAKKQQVASVD 270
HTH_18 pfam12833
Helix-turn-helix domain;
196-273 2.45e-24

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 96.89  E-value: 2.45e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502538741 196 LAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELL-RRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYR 273
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 396-622 3.59e-20

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 89.73  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 396 VFYLLGDVLALnvkpVGISDVQKGAAFEKELEGVQTLGTWFEPNPEAVLALDPDLIIA----PSEKIYQMMEKVAPTVYI 471
Cdd:pfam01497  10 ILYALGATDSI----VGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILstgyLTDEAEELLSLIIPTVIF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 472 PFDRM--TVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGilDKTVSIMEGGKGNMSVVSSkDYGRGSQIVY 549
Cdd:pfam01497  86 ESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAG-SNTYIGDLLR 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502538741 550 EyLGMKapaIVQAKLDKPSGeataESVSFEVLPQYAGDFVFRSAYEGMVDLSDNKV-----WNSIPAIKEGRLIEIDF 622
Cdd:pfam01497 163 I-LGIE---NIAAELSGSEY----APISFEAILSSNPDVIIVSGRDSFTKTGPEFVaanplWAGLPAVKNGRVYTLPS 232
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
147-274 5.20e-18

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 85.03  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 147 HVRALFYQVVYE-------------------LLRQMH-NPSLSRKPND-LAAQALGYIQENYAQPLSLEVLAELLDSSPR 205
Cdd:PRK10572  135 EFSDLFGQIEQAgqsegrysellamnllerlLLRCMEaIPESLHPPMDpRVREACQYISDHLASEFDIESVAQHVCLSPS 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502538741 206 HLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYRT 274
Cdd:PRK10572  215 RLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
 
Name Accession Description Interval E-value
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 383-629 9.16e-55

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 187.16  E-value: 9.16e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 383 GDVEIPVNPQRVVVFYLLGDVLALN-VKPVGISDVQKG--AAFEKELEGVQTLGTwfEPNPEAVLALDPDLIIAPS--EK 457
Cdd:cd01138     1 GEVEIPAKPKRIVALSGETEGLALLgIKPVGAASIGGKnpYYKKKTLAKVVGIVD--EPNLEKVLELKPDLIIVSSkqEE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 458 IYQMMEKVAPTVYIPFDRMTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGILDKTVSIMEGGKGNMsvVS 537
Cdd:cd01138    79 NYEKLSKIAPTVPVSYNSSDWEEQLKEIGKLLNKEDEAEKWLADYKQKAKEAKEKIKKKLGNDKSVAVLRGRKQIY--VF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 538 SKDYGRGSQIVYEYLGMKAPAIVQAKLDKPsgeaTAESVSFEVLPQYAGDFVFRSAY---EGMVDLSDNKVWNSIPAIKE 614
Cdd:cd01138   157 GEDGRGGGPILYADLGLKAPEKVKEIEDKP----GYAAISLEVLPEFDADYIFLLFFtgpEAKADFESLPIWKNLPAVKN 232

                         250
                  ....*....|....*
gi 2502538741 615 GRLIEIDFGLSYYND 629
Cdd:cd01138   233 NHVYIVDAWVFYFAD 247
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 321-621 1.66e-46

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 167.02  E-value: 1.66e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 321 KSSLATILFLCLTLILGACSAPTTTSTANPGAEQPQVnsaasastsnqpsakpatkiVSTAKGDVEIPVNPQRVVV--FY 398
Cdd:COG4594     2 KKLLLLLILLLALLLLAACGSSSSDSSSSEAAAGART--------------------VKHAMGETTIPGTPKRVVVleWS 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 399 LLGDVLALNVKPVGISDVQKG----AAFEKELEGVQTLGTWFEPNPEAVLALDPDLIIAPS---EKIYQMMEKVAPTV-- 469
Cdd:COG4594    62 FADALLALGVTPVGIADDNDYdrwvPYLRDLIKGVTSVGTRSQPNLEAIAALKPDLIIADKsrhEAIYDQLSKIAPTVlf 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 470 -YIPFDRMTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGiLDKTVSIMEGGKGNMSVVSSKDYgRGSqiV 548
Cdd:COG4594   142 kSRNGDYQENLESFKTIAKALGKEEEAEAVLADHDQRIAEAKAKLAAAD-KGKKVAVGQFRADGLRLYTPNSF-AGS--V 217

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2502538741 549 YEYLGMKAPaivqAKLDKPSGEATAEsVSFEVLPQYAGDFVFRSAYEGMV---DLSDNKVWNSIPAIKEGRLIEID 621
Cdd:COG4594   218 LAALGFENP----PKQSKDNGYGYSE-VSLEQLPALDPDVLFIATYDDPSilkEWKNNPLWKNLKAVKNGRVYEVD 288
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 390-632 5.42e-46

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 163.61  E-value: 5.42e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 390 NPQRVVV--FYLLGDVLALNVKPVGISDVQKGAAF----EKELEGVQTLGTWFEPNPEAVLALDPDLIIAPS---EKIYQ 460
Cdd:cd01146     2 KPQRIVAldWGALETLLALGVKPVGVADTAGYKPWipepALPLEGVVDVGTRGQPNLEAIAALKPDLILGSAsrhDEIYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 461 MMEKVAPTVYIPFDRMTVE--ERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGilDKTVSIMEGGKGNMSVVSS 538
Cdd:cd01146    82 QLSQIAPTVLLDSSPWLAEwkENLRLIAKALGKEEEAEKLLAEYDQRLAELRQKLPDKG--PKPVSVVRFSDAGSIRLYG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 539 KDYGRGSqiVYEYLGMKAPAIVQAKLDKPsgeatAESVSFEVLPQYAGDFVF---RSAYEGMVDLSDNKVWNSIPAIKEG 615
Cdd:cd01146   160 PNSFAGS--VLEDLGLQNPWAQETTNDSG-----FATISLERLAKADADVLFvftYEDEELAQALQANPLWQNLPAVKNG 232

                         250
                  ....*....|....*..
gi 2502538741 616 RLIEIDFGLSYYNDIYS 632
Cdd:cd01146   233 RVYVVDDVWWFFGGGLS 249
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 321-644 3.01e-37

ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 141.09  E-value: 3.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 321 KSSLATILFLCLTLILGACSAPTTTSTAnpgaeqpqvnsaasastsnqpSAKPATKIVSTAKGDVEIPVNPQRVVVFYL- 399
Cdd:COG4607     2 KKTLLAALALAAALALAACGSSSAAAAS---------------------AAAAETVTVEHALGTVEVPKNPKRVVVFDNg 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 400 -LgDVL-ALNVKPVGISDVQKGAAFEK-ELEGVQTLGTWFEPNPEAVLALDPDLIIA--PSEKIYQMMEKVAPTVYIPFD 474
Cdd:COG4607    61 aL-DTLdALGVEVAGVPKGLLPDYLSKyADDKYANVGTLFEPDLEAIAALKPDLIIIggRSAKKYDELSKIAPTIDLTVD 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 475 RM----TVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGildKTVSIMEGGkGNMSVvsskdYGRGSQ--IV 548
Cdd:COG4607   140 GEdyleSLKRNTETLGEIFGKEDEAEELVADLDAKIAALKAAAAGKG---TALIVLTNG-GKISA-----YGPGSRfgPI 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 549 YEYLGMKaPAivqaklDKPSGEAT-AESVSFEVLPQYAGDFVF---RSA-----YEGMVDLSDNKVWNSIPAIKEGRLIE 619
Cdd:COG4607   211 HDVLGFK-PA------DEDIEASThGQAISFEFIAEANPDWLFvidRDAaiggeGPAAKQVLDNELVKQTTAWKNGQIVY 283

                         330       340
                  ....*....|....*....|....*..
gi 2502538741 620 IDFGLSYYN--DIYSLDKQLDFIVDSL 644
Cdd:COG4607   284 LDPDAWYLAggGIQSLTEMLDEVADAL 310
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 393-650 3.56e-34

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 130.89  E-value: 3.56e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 393 RVVVFY--LLGDVLALNVKP--VGISDVQKGAAFEKELEGVQTLGTWFEPNPEAVLALDPDLIIAPS----EKIYQMMEK 464
Cdd:COG0614     2 RIVSLSpsATELLLALGAGDrlVGVSDWGYCDYPELELKDLPVVGGTGEPNLEAILALKPDLVLASSsgndEEDYEQLEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 465 V-APTVYIPFDRM-TVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGILDKTVSIMEGGKGNMSvvsskdYG 542
Cdd:COG0614    82 IgIPVVVLDPRSLeDLYESIRLLGELLGREERAEALIAEYEARLAAVRARLAGAEERPTVLYEIWSGDPLYT------AG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 543 RGS--QIVYEYLGMKAPAivqAKLDKPSGEataesVSFEVLPQYAGDFVFRSAYEGMVD--------LSDNKVWNSIPAI 612
Cdd:COG0614   156 GGSfiGELLELAGGRNVA---ADLGGGYPE-----VSLEQVLALDPDVIILSGGGYDAEtaeealeaLLADPGWQSLPAV 227

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2502538741 613 KEGRLIEIDFGLSYYNDIYSLDkQLDFIVDSLLKAAKK 650
Cdd:COG0614   228 KNGRVYVVPGDLLSRPGPRLLL-ALEDLAKALHPELFA 264
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 177-279 3.82e-31

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 123.73  E-value: 3.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 177 AQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYY 256
Cdd:COG4977   213 ARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292

                          90       100
                  ....*....|....*....|...
gi 2502538741 257 FAKMFKRYTGASPIRYRTEQARR 279
Cdd:COG4977   293 FRRAFRRRFGVSPSAYRRRFRAR 315
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
22-279 1.65e-29

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 117.57  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741  22 YLALFREEASRAWQLPASSFLFATKGRAEIWLDGQKHPAQRFYMLHGGKGARLQICPLEDVFEYYVIYYKALLPLPMNQE 101
Cdd:COG2207     1 LRLLILLLLLLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 102 LIAMLERQRPFDAAYGFLPEKAVCLLQNIQLMHEEWEKRNGLEHFHVRALFYQVVYELLRQMHNPSLSRKPNDLAAQALG 181
Cdd:COG2207    81 LLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 182 YIQENYAQpLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMF 261
Cdd:COG2207   161 LLLLLLLL-LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAF 239

                         250
                  ....*....|....*...
gi 2502538741 262 KRYTGASPIRYRTEQARR 279
Cdd:COG2207   240 KKRFGVTPSEYRKRLRAR 257
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 380-625 6.22e-29

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 116.20  E-value: 6.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 380 TAKGDVEIPVNPQRVVVF-YLLGDVL-ALNVKPVGISDVQKGAAFEKELEG--VQTLGTWFEPNPEAVLALDPDLIIAP- 454
Cdd:cd01140     1 HALGETKVPKNPEKVVVFdVGALDTLdALGVKVVGVPKSSTLPEYLKKYKDdkYANVGTLFEPDLEAIAALKPDLIIIGg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 455 --SEKIYQMmEKVAPTVYIPFD----RMTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEagilDKTVSIMEG 528
Cdd:cd01140    81 rlAEKYDEL-KKIAPTIDLGADlknyLESVKQNIETLGKIFGKEEEAKELVAEIDASIAEAKSAAKG----KKKALVVLV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 529 GKGNMSVvsskdYGRGSQI--VYEYLGMKaPAivqAKLDKPSGEatAESVSFEVLPQYAGDFVF---RSAYEGMVDLS-- 601
Cdd:cd01140   156 NGGKLSA-----FGPGSRFgwLHDLLGFE-PA---DENIKASSH--GQPVSFEYILEANPDWLFvidRGAAIGAEGSSak 224

                         250       260       270
                  ....*....|....*....|....*....|
gi 2502538741 602 ---DNKVWNSIPAIKEGRLIEID---FGLS 625
Cdd:cd01140   225 evlDNDLVKNTTAWKNGKVIYLDpdlWYLS 254
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
190-273 3.81e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 107.64  E-value: 3.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741  190 PLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASP 269
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2502538741  270 IRYR 273
Cdd:smart00342  81 SEYR 84
fecB PRK11411
iron-dicitrate transporter substrate-binding subunit; Provisional
 370-621 3.68e-26

iron-dicitrate transporter substrate-binding subunit; Provisional


Pssm-ID: 183123 [Multi-domain]  Cd Length: 303  Bit Score: 108.99  E-value: 3.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 370 SAKPATkiVSTAKGDVEIPVNPQRVVVF-YLLGDVLA-LNVKPVGISDVQKG----AAFEKELEGVQTLGTWFEPNPEAV 443
Cdd:PRK11411   20 HAFAVT--VQDEQGTFTLEKTPQRIVVLeLSFVDALAaVGVSPVGVADDNDAkrilPEVRAHLKPWQSVGTRSQPSLEAI 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 444 LALDPDLIIAPSEK---IYQMMEKVAPTVYIPFDRMTVEERLQ---KLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAg 517
Cdd:PRK11411   98 AALKPDLIIADSSRhagVYIALQKIAPTLLLKSRNETYQENLQsaaIIGEVLGKKREMQARIEQHKERMAQFASQLPKG- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 518 ildKTVSIMEGGKGNMSVVSSKDYGrGSqiVYEYLGMKAPAivqakldKPSGEATAESVSFEVLPQYAGDFVFRSAY--E 595
Cdd:PRK11411  177 ---TRVAFGTSREQQFNLHSPESYT-GS--VLAALGLNVPK-------APMNGAAMPSISLEQLLALNPDWLLVAHYrqE 243

                         250       260
                  ....*....|....*....|....*..
gi 2502538741 596 GMVD-LSDNKVWNSIPAIKEGRLIEID 621
Cdd:PRK11411  244 SIVKrWQQDPLWQMLTAAKKQQVASVD 270
HTH_18 pfam12833
Helix-turn-helix domain;
196-273 2.45e-24

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 96.89  E-value: 2.45e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502538741 196 LAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELL-RRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYR 273
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 174-280 1.70e-21

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 96.66  E-value: 1.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 174 DLAAQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLrRTEASLQDIAEEIGYPD 253
Cdd:COG2169    84 DLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGS 162

                          90       100
                  ....*....|....*....|....*..
gi 2502538741 254 RYYFAKMFKRYTGASPIRYRTEQARRD 280
Cdd:COG2169   163 LSRFYEAFKKLLGMTPSAYRRGGAGAA 189
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 396-622 3.59e-20

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 89.73  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 396 VFYLLGDVLALnvkpVGISDVQKGAAFEKELEGVQTLGTWFEPNPEAVLALDPDLIIA----PSEKIYQMMEKVAPTVYI 471
Cdd:pfam01497  10 ILYALGATDSI----VGVDAYTRDPLKADAVAAIVKVGAYGEINVERLAALKPDLVILstgyLTDEAEELLSLIIPTVIF 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 472 PFDRM--TVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGilDKTVSIMEGGKGNMSVVSSkDYGRGSQIVY 549
Cdd:pfam01497  86 ESSSTgeSLKEQIKQLGELLGLEDEAEELVAEIDSALAAAKKAVPSLT--RKPVLVFGGADGGGYVVAG-SNTYIGDLLR 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502538741 550 EyLGMKapaIVQAKLDKPSGeataESVSFEVLPQYAGDFVFRSAYEGMVDLSDNKV-----WNSIPAIKEGRLIEIDF 622
Cdd:pfam01497 163 I-LGIE---NIAAELSGSEY----APISFEAILSSNPDVIIVSGRDSFTKTGPEFVaanplWAGLPAVKNGRVYTLPS 232
TroA-like cd00636
Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function ...
 392-528 1.33e-18

Helical backbone metal receptor (TroA-like domain). These proteins have been shown to function in the ABC transport of ferric siderophores and metal ions such as Mn2+, Fe3+, Cu2+ and/or Zn2+. Their ligand binding site is formed in the interface between two globular domains linked by a single helix. Many of these proteins also possess a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence). The TroA-like proteins differ in their fold and ligand-binding mechanism from the PBPI and PBPII proteins, but are structurally similar, however, to the beta-subunit of the nitrogenase molybdenum-iron protein MoFe. Most TroA-like proteins are encoded by ABC-type operons and appear to function as periplasmic components of ABC transporters in metal ion uptake.


Pssm-ID: 238347 [Multi-domain]  Cd Length: 148  Bit Score: 82.99  E-value: 1.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 392 QRVVV-FYLLGDV---LALNVKPVGISDVQKGAAFEKE-LEGVQTLGTWFEPNPEAVLALDPDLIIAPS---EKIYQMME 463
Cdd:cd00636     1 KRVVAlDPGATELllaLGGDDKPVGVADPSGYPPEAKAlLEKVPDVGHGYEPNLEKIAALKPDLIIANGsglEAWLDKLS 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 464 KVA-PTVYIPFDRM----TVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLgeAGILDKTVSIMEG 528
Cdd:cd00636    81 KIAiPVVVVDEASElsleNIKESIRLIGKALGKEENAEELIAELDARLAELRAKL--AKIPKKKVSLVVG 148
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
147-274 5.20e-18

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 85.03  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 147 HVRALFYQVVYE-------------------LLRQMH-NPSLSRKPND-LAAQALGYIQENYAQPLSLEVLAELLDSSPR 205
Cdd:PRK10572  135 EFSDLFGQIEQAgqsegrysellamnllerlLLRCMEaIPESLHPPMDpRVREACQYISDHLASEFDIESVAQHVCLSPS 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2502538741 206 HLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYRT 274
Cdd:PRK10572  215 RLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 369-623 1.33e-17

Periplasmic binding protein TroA_e. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 83.56  E-value: 1.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 369 PSAKPATKIVSTAKG-DVEIPVNPQRVVVFYLLGDVLALNVKP-----VGISDVQKGAAFEK---ELEGVQTLGTWFEPN 439
Cdd:cd01142     1 PAATAATRTITDMAGrKVTIPDEVKRIAALWGAGNAVVAALGGgklivATTSTVQQEPWLYRlapSLENVATGGTGNDVN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 440 PEAVLALDPDLIIAPS---EKIYQMMEKVAPTVYIPFDRM-TVEERLQKLGEVLGKEGESKKL---LSDFHAKVAESKKK 512
Cdd:cd01142    81 IEELLALKPDVVIVWStdgKEAGKAVLRLLNALSLRDAELeEVKLTIALLGELLGRQEKAEALvayFDDNLAYVAARTKK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 513 LGEagilDKTVSIMEGGKGNMSVVsskdyGRGSqIVYEYLGMkAPAI--VQAKLDKPSGEataesVSFEVLPQYAGDFVF 590
Cdd:cd01142   161 LPD----SERPRVYYAGPDPLTTD-----GTGS-ITNSWIDL-AGGInvASEATKKGSGE-----VSLEQLLKWNPDVII 224

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2502538741 591 RSAYEGMVDLSDNKVWNSIPAIKEGRLIEIDFG 623
Cdd:cd01142   225 VGNADTKAAILADPRWQNLRAVKNGRVYVNPEG 257
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
151-282 1.69e-16

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 80.11  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 151 LFYQVVYELLRQMHNPSLSRkpNDLAAQAL-GYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRME 229
Cdd:PRK13503  149 LFMQLLVLLRKSSLQENGEN--SDARLNQLlAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLL 226

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2502538741 230 KAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPiryRTEQARRDET 282
Cdd:PRK13503  227 KARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSP---RDIRQGRDGF 276
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 387-617 2.51e-14

Metal binding protein HemV-2. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 73.52  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 387 IPVNPQRVVVfylLGD-----VLALNV--KPVGISDVQK---GAAFE------KELEGVQTLGTWFEPNPEAVLALDPDL 450
Cdd:cd01147     1 VPKPVERVVA---AGPgalrlLYALAApdKIVGVDDAEKsdeGRPYFlaspelKDLPVIGRGGRGNTPNYEKIAALKPDV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 451 IIAP----SEKIYQMMEKVA--PTVYI--PFDRMTVEERLQKLGEVLGKEGESKKLLS---DFHAKVAESKKKLGEAGIl 519
Cdd:cd01147    78 VIDVgsddPTSIADDLQKKTgiPVVVLdgGDSLEDTPEQIRLLGKVLGKEERAEELISfieSILADVEERTKDIPDEEK- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 520 dKTVSIMEGGKGNMSVVSSKdyGRGSQIVYEYLGMKapAIVQAKldkpsGEATAESVSFEVLPQYAGDFVF---RSAYE- 595
Cdd:cd01147   157 -PTVYFGRIGTKGAAGLESG--LAGSIEVFELAGGI--NVADGL-----GGGGLKEVSPEQILLWNPDVIFldtGSFYLs 226

                         250       260
                  ....*....|....*....|..
gi 2502538741 596 GMVDLSDNKVWNSIPAIKEGRL 617
Cdd:cd01147   227 LEGYAKNRPFWQSLKAVKNGRV 248
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
130-279 5.28e-13

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 69.93  E-value: 5.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 130 IQLMHEEWEKRNGLEHFHVRALFYQVVYELLRQMHNPSLSRK-PN----DLAAQALgyiQENYAQPLSLEVLAELLDSSP 204
Cdd:PRK13501  130 IQQLAQESRKTDSWSIQLTEVLLLQLAIVLKRHRYRAEQAHLlPDgeqlDLIMSAL---QQSLGAYFDMADFCHKNQLVE 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502538741 205 RHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYRTEQARR 279
Cdd:PRK13501  207 RSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRS 281
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 372-512 1.54e-12

Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238563 [Multi-domain]  Cd Length: 195  Bit Score: 66.53  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 372 KPATKIVSTAKGDVEIpvnpqrvvVFYL-LGDvlalnvKPVGISDVQkgaAFEKELEGVQTLGTWFEPNPEAVLALDPDL 450
Cdd:cd01143     1 KEPERIVSLSPSITEI--------LFALgAGD------KIVGVDTYS---NYPKEVRKKPKVGSYSNPNVEKIVALKPDL 63

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2502538741 451 IIA----PSEKIYQMMEKVAPTVYIPFDRM--TVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKK 512
Cdd:cd01143    64 VIVssssLAELLEKLKDAGIPVVVLPAASSldEIYDQIELIGKITGAEEEAEKLVKEMKQKIDKVKDK 131
PRK10957 PRK10957
iron-enterobactin transporter periplasmic binding protein; Provisional
 359-513 3.09e-12

iron-enterobactin transporter periplasmic binding protein; Provisional


Pssm-ID: 236806 [Multi-domain]  Cd Length: 317  Bit Score: 68.08  E-value: 3.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 359 SAASASTSNQPsakpatKIVSTAKGDVEIPVNPQRVV--VFYLLGDVLALNVKPVG------ISDVQKGAAF------EK 424
Cdd:PRK10957   18 AAAQASAAGWP------RTVTDSRGSVTLESKPQRIVstSVTLTGTLLAIDAPVIAsgattpNTRVADDQGFfrqwsdVA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 425 ELEGVQTLgtW-FEPNPEAVLALDPDLIIAPSE------KIYQMMEKVAPTVYIPFDRMTVEERLQKLGEVLGKEGESKK 497
Cdd:PRK10957   92 KERGVEVL--YiGEPDAEAVAAQMPDLIVISATggdsalALYDQLSAIAPTLVIDYDDKSWQELATQLGEATGLEKQAAA 169

                         170
                  ....*....|....*.
gi 2502538741 498 LLSDFHAKVAESKKKL 513
Cdd:PRK10957  170 VIAQFDAQLAEVKAKI 185
PRK10371 PRK10371
transcriptional regulator MelR;
161-273 3.10e-12

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 67.92  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 161 RQMHNPSLSRKPNDLAAQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEA 240
Cdd:PRK10371  178 SRTHKNSVSRHAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDK 257

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2502538741 241 SLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYR 273
Cdd:PRK10371  258 SILDIALTAGFRSSSRFYSTFGKYVGMSPQQYR 290
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
168-273 1.64e-11

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 62.04  E-value: 1.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 168 LSRKPNDLAA--QALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDI 245
Cdd:PRK11511    1 MSRRNTDAITihSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYL 80

                          90       100
                  ....*....|....*....|....*...
gi 2502538741 246 AEEIGYPDRYYFAKMFKRYTGASPIRYR 273
Cdd:PRK11511   81 AERYGFESQQTLTRTFKNYFDVPPHKYR 108
ftrA PRK09393
transcriptional activator FtrA; Provisional
 168-273 1.90e-11

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 65.76  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 168 LSRKPNDLAAQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAE 247
Cdd:PRK09393  212 VASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAE 291

                          90       100
                  ....*....|....*....|....*.
gi 2502538741 248 EIGYPDRYYFAKMFKRYTGASPIRYR 273
Cdd:PRK09393  292 RAGFGSEESLRHHFRRRAATSPAAYR 317
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
182-273 8.73e-11

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 59.17  E-value: 8.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 182 YIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMF 261
Cdd:PRK10219   13 WIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVF 92

                          90
                  ....*....|..
gi 2502538741 262 KRYTGASPIRYR 273
Cdd:PRK10219   93 RRQFDRTPSDYR 104
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
131-280 1.45e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 59.68  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 131 QLMHEEwEKRNGLEHFHVRALFYQVVYELLRQMHN----PSLSRKpnDLAAQALGYIQENYAQPLSLEVLAELLDSSPRH 206
Cdd:PRK13502  132 QLEHES-NGRDPLANEMAELLFGQLVMTLKRHRYAtddlPATSRE--TLLDKLITALANSLECPFALDAFCQQEQCSERV 208

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2502538741 207 LSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYRTEQARRD 280
Cdd:PRK13502  209 LRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQSD 282
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
151-280 5.80e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 58.19  E-value: 5.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 151 LFYQVVYELLRQMHNpSLSRKPND---LAAQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLR 227
Cdd:PRK13500  181 LFGQLVMLLNRHRYT-SDSLPPTSsetLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVR 259

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2502538741 228 MEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYRTEQARRD 280
Cdd:PRK13500  260 VCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRHLNSQKD 312
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 391-621 7.08e-08

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 54.27  E-value: 7.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 391 PQRVV--------VFYLLGdvLALNVKPVGISDVQKGAAFEKELEGVQTLGTwFEPNPEAVLALDPDLIIApsEKIYQMM 462
Cdd:cd01148    18 PQRVVsndqntteMMLALG--LQDRMVGTAGIDNKDLPELKAKYDKVPELAK-KYPSKETVLAARPDLVFG--GWSYGFD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 463 EKVAPT----------VYIP-------FDRMTVE---ERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKLGEAGILDKT 522
Cdd:cd01148    93 KGGLGTpdslaelgikTYILpescgqrRGEATLDdvyNDIRNLGKIFDVEDRADKLVADLKARLAEISAKVKGDGKKVAV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 523 VSIMEGGKGNMSvvsskdYGRGS--QIVYEYLGMKApaiVQAKLDKPSGEATAESVSfEVLPQY--AGDFVFRSAYEGMV 598
Cdd:cd01148   173 FVYDSGEDKPFT------SGRGGipNAIITAAGGRN---VFADVDESWTTVSWETVI-ARNPDVivIIDYGDQNAAEQKI 242

                         250       260
                  ....*....|....*....|....
gi 2502538741 599 D-LSDNKVWNSIPAIKEGRLIEID 621
Cdd:cd01148   243 KfLKENPALKNVPAVKNNRFIVLP 266
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
189-272 1.31e-07

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 54.03  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 189 QPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEaSLQDIAEEIGYPD--RYY---------F 257
Cdd:PRK15435   98 TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSILNAGFPDssSYYrkadetlgmT 176

                          90
                  ....*....|....*
gi 2502538741 258 AKMFKRYTGASPIRY 272
Cdd:PRK15435  177 AKQFRHGGENLAVRY 191
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 183-222 3.87e-07

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 46.76  E-value: 3.87e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2502538741 183 IQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEY 222
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQY 40
ChuT COG4558
ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism] ...
 422-545 2.11e-06

ABC-type hemin transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443619 [Multi-domain]  Cd Length: 285  Bit Score: 49.80  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 422 FEKELEGVQTLGTWFEPNPEAVLALDPDLIIA-----PSEKIYQMMEKVAPTVYIPfDRMTVE---ERLQKLGEVLGKEG 493
Cdd:COG4558    59 YPAAAKALPDVGYMRQLSAEGILSLKPTLVLAsegagPPEVLDQLRAAGVPVVVVP-AAPSLEgvlAKIRAVAAALGVPE 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2502538741 494 ESKKLLSDFHAKVAESKKKLGEAGILDKTVSIMEGGKGNMSVvsskdYGRGS 545
Cdd:COG4558   138 AGEALAARLEADLAALAARVAAIGKPPRVLFLLSRGGGRPMV-----AGRGT 184
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 159-273 4.74e-06

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 48.87  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 159 LLR---QMHNPSLSRKPNDLAaQALGYIQENYAQP-LSLEVLAELLDSSPRHLSRLFkQRTGSSPIEYMISLRMEKAKEL 234
Cdd:PRK09685  180 LLRpalHQRESVQPRRERQFQ-KVVALIDQSIQEEiLRPEWIAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLDRCADD 257

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2502538741 235 LRR--TEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRYR 273
Cdd:PRK09685  258 LRPaaDDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYR 298
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 238-274 7.87e-06

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 42.91  E-value: 7.87e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2502538741 238 TEASLQDIAEEIGYpDRYYFAKMFKRYTGASPIRYRT 274
Cdd:pfam00165   7 TNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 384-632 1.27e-05

Periplasmic binding protein TroA_f. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 47.69  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 384 DVEIPVNPQRVVV-FYLLGDVLALnVKP-------VG------ISDVQKGAAFEK---ELEGVQTLGTWFEP--NPEAVL 444
Cdd:cd01139    10 KVTLDAPVERVLLgEGRQLYALAL-LEGenpfariVGwggdlkKGDPDTYAKYKEkfpEIADIPLIGSTYNGdfSVEKVL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 445 ALDPDLIIAPSE--------KIYQMMEKVA-PTVYIPFdRMTVEERLQK----LGEVLGKEGESKKLLSDFHAKVAESKK 511
Cdd:cd01139    89 TLKPDLVILNIWakttaeesGILEKLEQAGiPVVFVDF-RQKPLKNTTPsmrlLGKALGREERAEEFIEFYQERIDRIRD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 512 KLGEAGILDKTVSIMEGGKGnmsvvsSKDYGR--GSQIVYEYLGmKAPA--IVQAKLDKPSGEATAESV----------- 576
Cdd:cd01139   168 RLAKINEPKPKVFIELGAGG------PEECCStyGNGNWGELVD-AAGGdnIADGLIPGTSGELNAEYViaanpeiiiat 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2502538741 577 ---------SFEVLPQYAGDfvfRSAYEGMVDLSDNKVWNSIPAIKEGRLIEIDFGlsYYNDIYS 632
Cdd:cd01139   241 ggnwakdpsGVSLGPDGTTA---DAKESLLRALLKRPGWSSLQAVKNGRVYALWHQ--FYRSPYN 300
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 188-275 3.02e-05

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 46.23  E-value: 3.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 188 AQPLSLEVLAELLDSSPRHLSRLFKQRTgSSPIEYMISLRMEKAKELLRrTEASLQDIAEEIGYPDRYYFAKMFKRYTGA 267
Cdd:PRK09940  148 AHPWKLKDICDCLYISESLLKKKLKQEQ-TTFSQILLDARMQHAKNLIR-VEGSVNKIAEQCGYASTSYFIYAFRKHFGN 225


                  ....*...
gi 2502538741 268 SPIRYRTE 275
Cdd:PRK09940  226 SPKRVSKE 233
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 192-273 7.16e-05

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 45.13  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 192 SLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIR 271
Cdd:PRK10296  190 ALENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGS 269


                  ..
gi 2502538741 272 YR 273
Cdd:PRK10296  270 YR 271
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 174-278 1.49e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 44.15  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 174 DLAAQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFkQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPD 253
Cdd:PRK09978  142 NMRTRVCTVINNNIAHEWTLARIASELLMSPSLLKKKL-REEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHS 220

                          90       100
                  ....*....|....*....|....*
gi 2502538741 254 RYYFAKMFKRYTGASPIRYRTEQAR 278
Cdd:PRK09978  221 VSYFIYVFRNYYGMTPTEYQERSAQ 245
PRK10576 PRK10576
Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;
388-513 1.55e-04

Fe(3+)-hydroxamate ABC transporter substrate-binding protein FhuD;


Pssm-ID: 236719  Cd Length: 292  Bit Score: 44.23  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 388 PVNPQRVVVFY-----LLgdvLALNVKPVGISDVQKGAAFEKELE---GVQTLGTWFEPNPEAVLALDPDLII-----AP 454
Cdd:PRK10576   29 AIDPNRIVALEwlpveLL---LALGVTPYGVADTHNYRLWVSEPAlpdSVIDVGLRTEPNLELLTQMKPSLILwsagyGP 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2502538741 455 SEkiyQMMEKVAPTVYIPF-DR----MTVEERLQKLGEVLGKEGESKKLLSDFHAKVAESKKKL 513
Cdd:PRK10576  106 SP---EKLARIAPGRGFAFsDGkkplAVARKSLVELAQRLNLEAAAETHLAQFDDFIASAKPRL 166
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
180-273 1.62e-04

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 44.23  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 180 LGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTGSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAK 259
Cdd:PRK15121   11 LIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQTFTR 90

                          90
                  ....*....|....
gi 2502538741 260 MFKRYTGASPIRYR 273
Cdd:PRK15121   91 AFKKQFAQTPALYR 104
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 144-272 2.79e-04

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 43.52  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 144 EHFHVRALFYQVVYE-----LLRQMHNpslsrkpNDLAAQALGYIQENYAQPLSLEVLAELLDSSPRHLSRLFKQRTgSS 218
Cdd:PRK15186  153 KEYLIRFLLSEFIYEpeafaLFRELSQ-------NTLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQEN-TS 224

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2502538741 219 PIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASPIRY 272
Cdd:PRK15186  225 FSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
HutB cd01149
Hemin binding protein HutB. These proteins have been shown to function as initial receptors ...
 422-512 5.51e-04

Hemin binding protein HutB. These proteins have been shown to function as initial receptors in ABC transport of hemin and hemoproteins in many eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains.


Pssm-ID: 238569 [Multi-domain]  Cd Length: 235  Bit Score: 41.87  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 422 FEKELEGVQTLGTWFEPNPEAVLALDPDLIIA-----PSEKIYQMMEKVAPTVYIP--FDRMTVEERLQKLGEVLGKEGE 494
Cdd:cd01149    33 YPEAAAKLPDVGYMRQLSAEGVLSLKPTLVIAsdeagPPEALDQLRAAGVPVVTVPstPTLDGLLTKIRQVAQALGVPEK 112

                          90
                  ....*....|....*...
gi 2502538741 495 SKKLLSDFHAKVAESKKK 512
Cdd:cd01149   113 GEALAQEVRQRLAALRKT 130
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 392-621 1.71e-03

Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238564 [Multi-domain]  Cd Length: 245  Bit Score: 40.75  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 392 QRVV--------VFYLLGdvlaLNVKPVGISDvqkGAAFEKELEGVQTLGTWFEPNPEAVLALDPDLIIA----PSEKIY 459
Cdd:cd01144     1 MRIVslapsateLLYALG----LGDQLVGVTD---YCDYPPEAKKLPRVGGFYQLDLERVLALKPDLVIAwddcNVCAVV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 460 QMMEKVAPTVYIpFDRMTVEERLQ---KLGEVLGKEGESKKLLSDFHAKVAESKKKlgEAGILDKTVSIMEGGKGNMSVv 536
Cdd:cd01144    74 DQLRAAGIPVLV-SEPQTLDDILAdirRLGTLAGRPARAEELAEALRRRLAALRKQ--YASKPPPRVFYQEWIDPLMTA- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 537 sskdygrGSQIVYEYLGMKAPAIVQAKLDKPSGEATAESVSFE-----VLPQYAGDFVFrsayegmVDLSDNKVWNSIPA 611
Cdd:cd01144   150 -------GGDWVPELIALAGGVNVFADAGERSPQVSWEDVLAAnpdviVLSPCGFGFTP-------AILRKEPAWQALPA 215

                         250
                  ....*....|
gi 2502538741 612 IKEGRLIEID 621
Cdd:cd01144   216 VRNGRVYAVD 225
TroA_d cd01141
Periplasmic binding protein TroA_d. These proteins are predicted to function as initial ...
 387-513 1.87e-03

Periplasmic binding protein TroA_d. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238561 [Multi-domain]  Cd Length: 186  Bit Score: 39.71  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2502538741 387 IPVNPQRVVVFYLLGDVLALNV----KPVGISD---VQKGAAFEKELEgvQTLGTWFEPNPEAVLALDPDLII----APS 455
Cdd:cd01141     4 IKVPPKRIVVLSPTHVDLLLALdkadKIVGVSAsayDLNTPAVKERID--IQVGPTGSLNVELIVALKPDLVIlyggFQA 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2502538741 456 EKIYQMMEKVA-PTVYIPF--DRMTVEERLQKLGEVLGKEGESKKllSDFHAKVAESKKKL 513
Cdd:cd01141    82 QTILDKLEQLGiPVLYVNEypSPLGRAEWIKFAAAFYGVGKEDKA--DEAFAQIAGRYRDL 140
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 216-269 6.55e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 39.21  E-value: 6.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2502538741 216 GSSPIEYMISLRMEKAKELLRRTEASLQDIAEEIGYPDRYYFAKMFKRYTGASP 269
Cdd:PRK15185  247 GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTP 300
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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