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Conserved domains on  [gi|498163171|ref|WP_010477327|]
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phosphate ABC transporter substrate-binding/OmpA family protein [Acaryochloris sp. CCMEE 5410]

Protein Classification

phosphate ABC transporter substrate-binding/OmpA family protein( domain architecture ID 10402912)

fused phosphate ABC transporter substrate-binding protein/OmpA family membrane protein contains an N-terminal domain similar to Bacillus subtilis phosphate-binding protein PstS, part of the ABC transporter complex PstSACB that is involved in phosphate import, and a C-terminal domain that may act as a porin with low permeability that allows slow penetration of small solutes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 413-514 4.07e-24

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


:

Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 96.85  E-value: 4.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 413 VKFAVGAADLTTTGRQTLDKLSKEIAEfNPDTvAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGK 491
Cdd:cd07185    4 IYFDFGSAELTPEAKPLLDKLAEVLKK-NPDA-KIRIEGHTDSRGSDAYNQELSERRAEAVADYLVSKGVDASrITAVGY 81

                         90       100
                 ....*....|....*....|....*
gi 498163171 492 GFSTPL-PGISPAD-ARNQRTEIRL 514
Cdd:cd07185   82 GESRPIaSNDTEEGrAKNRRVEIVI 106
OmpA COG2885
Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall ...
 274-516 5.32e-24

Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442131 [Multi-domain]  Cd Length: 294  Bit Score: 102.17  E-value: 5.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 274 RIESGISNTSQLQDQIANDGDLAASDADTVLKGINFFTALETQGWMQQETLNERIRATAAVLVLSGNLTQVPDDPAQLYD 353
Cdd:COG2885   50 SAGAAGGAAAGAEAGGLSAGLELLDAGSLSATAAAGAAALLVLLAALGALGAGLAALLLAIAAAASAAAADALALAAGAA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 354 PQFVSQAAENTKKLIDIVRADNPELAQKLEGKTTAPTAAKPTADIKSAPSIGNLKVRGEVKFAVGAADLTTTGRQTLDKL 433
Cdd:COG2885  130 AALGALGASAAAAAAALAAAKALGDSAAAALDAAAKAEAAAAAAALLPAAVAEVVLLSNVYFDFDSAELTPEAKAALDEL 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 434 SKEIAEfNPDTVaVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGKGFSTPLPGISPADAR--NQRT 510
Cdd:COG2885  210 AALLKE-NPDLR-IEIEGHTDSRGSDAYNLALSERRAEAVKDYLVSKGIPASrITAVGYGESRPVASNDTEEGRakNRRV 287


                 ....*.
gi 498163171 511 EIRLVR 516
Cdd:COG2885  288 EIVVLK 293
Periplasmic_Binding_Protein_Type_2 super family cl21456
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ...
 94-273 3.53e-21

Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences.


The actual alignment was detected with superfamily member cd13563:

Pssm-ID: 473866 [Multi-domain]  Cd Length: 208  Bit Score: 91.53  E-value: 3.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  94 QRAQALGQGKADFIVTTLDQFLKQKPKG---KIVGLIDRTVGADAVVLNtrqfPQLKSLINLsqlvkqgKSKQYSIVYAG 170
Cdd:cd13563   41 DSMAALASGQIDAAATTLDDALAMAAKGvpvKIVLVLDNSNGADGIVAK----PGIKSIADL-------KGKTVAVEEGS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 171 dtpSEYLALVLDTKFDAFNLSDFRVIKVE--DASQAWklmqdTKENVAIAVLWEPFVSQARKQGHTVVL-SSKDAPNTIV 247
Cdd:cd13563  110 ---VSHFLLLNALEKAGLTEKDVKIVNMTagDAGAAF-----IAGQVDAAVTWEPWLSNALKRGKGKVLvSSADTPGLIP 181

                        170       180
                 ....*....|....*....|....*.
gi 498163171 248 DVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:cd13563  182 DVLVVREDFIKKNPEAVKAVVKAWFD 207
 
Name Accession Description Interval E-value
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 413-514 4.07e-24

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 96.85  E-value: 4.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 413 VKFAVGAADLTTTGRQTLDKLSKEIAEfNPDTvAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGK 491
Cdd:cd07185    4 IYFDFGSAELTPEAKPLLDKLAEVLKK-NPDA-KIRIEGHTDSRGSDAYNQELSERRAEAVADYLVSKGVDASrITAVGY 81

                         90       100
                 ....*....|....*....|....*
gi 498163171 492 GFSTPL-PGISPAD-ARNQRTEIRL 514
Cdd:cd07185   82 GESRPIaSNDTEEGrAKNRRVEIVI 106
OmpA COG2885
Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall ...
 274-516 5.32e-24

Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442131 [Multi-domain]  Cd Length: 294  Bit Score: 102.17  E-value: 5.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 274 RIESGISNTSQLQDQIANDGDLAASDADTVLKGINFFTALETQGWMQQETLNERIRATAAVLVLSGNLTQVPDDPAQLYD 353
Cdd:COG2885   50 SAGAAGGAAAGAEAGGLSAGLELLDAGSLSATAAAGAAALLVLLAALGALGAGLAALLLAIAAAASAAAADALALAAGAA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 354 PQFVSQAAENTKKLIDIVRADNPELAQKLEGKTTAPTAAKPTADIKSAPSIGNLKVRGEVKFAVGAADLTTTGRQTLDKL 433
Cdd:COG2885  130 AALGALGASAAAAAAALAAAKALGDSAAAALDAAAKAEAAAAAAALLPAAVAEVVLLSNVYFDFDSAELTPEAKAALDEL 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 434 SKEIAEfNPDTVaVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGKGFSTPLPGISPADAR--NQRT 510
Cdd:COG2885  210 AALLKE-NPDLR-IEIEGHTDSRGSDAYNLALSERRAEAVKDYLVSKGIPASrITAVGYGESRPVASNDTEEGRakNRRV 287


                 ....*.
gi 498163171 511 EIRLVR 516
Cdd:COG2885  288 EIVVLK 293
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
 94-273 3.53e-21

Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270281 [Multi-domain]  Cd Length: 208  Bit Score: 91.53  E-value: 3.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  94 QRAQALGQGKADFIVTTLDQFLKQKPKG---KIVGLIDRTVGADAVVLNtrqfPQLKSLINLsqlvkqgKSKQYSIVYAG 170
Cdd:cd13563   41 DSMAALASGQIDAAATTLDDALAMAAKGvpvKIVLVLDNSNGADGIVAK----PGIKSIADL-------KGKTVAVEEGS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 171 dtpSEYLALVLDTKFDAFNLSDFRVIKVE--DASQAWklmqdTKENVAIAVLWEPFVSQARKQGHTVVL-SSKDAPNTIV 247
Cdd:cd13563  110 ---VSHFLLLNALEKAGLTEKDVKIVNMTagDAGAAF-----IAGQVDAAVTWEPWLSNALKRGKGKVLvSSADTPGLIP 181

                        170       180
                 ....*....|....*....|....*.
gi 498163171 248 DVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:cd13563  182 DVLVVREDFIKKNPEAVKAVVKAWFD 207
OmpA pfam00691
OmpA family; The Pfam entry also includes MotB and related proteins which are not included in ...
 415-509 7.79e-17

OmpA family; The Pfam entry also includes MotB and related proteins which are not included in the Prosite family.


Pssm-ID: 425825 [Multi-domain]  Cd Length: 95  Bit Score: 75.86  E-value: 7.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  415 FAVGAADLTTTGRQTLDKLSKEIaEFNPDTVAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGI-KQTIQAEGKGF 493
Cdd:pfam00691   1 FDPGSSQLTPKAKATLDEIADLL-KFPELKNTITIEGHTDTVGSAAYNWELSQRRAEAVRRYLVNFGVpPSRISVVGYGA 79

                          90
                  ....*....|....*.
gi 498163171  494 STPLPGISPADARNQR 509
Cdd:pfam00691  80 TKPITDNKTPEGRARN 95
PRK10808 PRK10808
outer membrane protein A; Reviewed
 371-499 6.26e-15

outer membrane protein A; Reviewed


Pssm-ID: 236764 [Multi-domain]  Cd Length: 351  Bit Score: 76.27  E-value: 6.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 371 VRADNPELA--------QKLEGKTTAPTAA-KPTADIKSapsignLKVRGEVKFAVGAADLTTTGRQTLDKLSKEIAEFN 441
Cdd:PRK10808 181 ARPDNGMLSvgvsyrfgQEEAAPVVAPAPApAPVVQTKH------FTLKSDVLFNFNKATLKPEGQQALDQLYSQLSNLD 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498163171 442 PDTVAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGI-KQTIQAEGKGFSTPLPG 499
Cdd:PRK10808 255 PKDGSVVVLGYTDRIGSDAYNQGLSEKRAQSVVDYLVSKGIpADKISARGMGKSNPVTG 313
MotB COG1360
Flagellar motor protein MotB [Cell motility];
407-516 1.17e-13

Flagellar motor protein MotB [Cell motility];


Pssm-ID: 440971 [Multi-domain]  Cd Length: 174  Bit Score: 69.10  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 407 LKVRGEVKFAVGAADLTTTGRQTLDKLSKEIAEFNpdtVAVRVIGHTS----KTGSASLNQTLSQQRAQVVVQYLKQLGI 482
Cdd:COG1360   55 IEIQDRVLFDSGSAELTPEGRELLDKIAAVLAEVP---NRIRVEGHTDnvpiSTARFPSNWELSAARAAAVVRYLIEGGV 131

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 498163171 483 KQT-IQAEGKGFSTPL-PGISP-ADARNQRTEIRLVR 516
Cdd:COG1360  132 PPErLSAVGYGDTRPLaPNDTPeGRARNRRVEIVILR 168
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
 94-345 2.32e-13

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 70.80  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  94 QRAQALGQGKADFIVTTLDQFLKQKPKG---KIVGLIDRTVGADAVVLNTRQFPQLKSLinlsqlvkQGKSkqysIVYAG 170
Cdd:COG0715   63 AALEALAAGQADFGVAGAPPALAARAKGapvKAVAALSQSGGNALVVRKDSGIKSLADL--------KGKK----VAVPG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 171 DTPSEY-LALVLDTkfDAFNLSDFRVIKVEDASQAWKLMQDtkeNVAIAVLWEPFVSQARKQG--HTVVLSSKDAPNTIV 247
Cdd:COG0715  131 GSTSHYlLRALLAK--AGLDPKDVEIVNLPPPDAVAALLAG---QVDAAVVWEPFESQAEKKGggRVLADSADLVPGYPG 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 248 DVLVASDKVIQSQPEQISAFLAAYYRRIESGISNTSQLQDQIANDGDLAASDADTVLKGinFFTALETQGWMQQetlnER 327
Cdd:COG0715  206 DVLVASEDFLEENPEAVKAFLRALLKAWAWAAANPDEAAAILAKATGLDPEVLAAALEG--DLRLDPPLGAPDP----AR 279

                        250
                 ....*....|....*...
gi 498163171 328 IRATAAVLVLSGNLTQVP 345
Cdd:COG0715  280 LQRVADFLVELGLLPKDV 297
NMT1 pfam09084
NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ...
 73-273 8.04e-05

NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine.3]. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.


Pssm-ID: 430398 [Multi-domain]  Cd Length: 216  Bit Score: 44.13  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171   73 FQEAlgepGIRLDYADEFDQFQRAQALGQGKADFIVTTLDQFLKQKPKG-KIVG---LIDRTVGAdAVVLNTRQFPQLKS 148
Cdd:pfam09084  16 FKEE----GLDVEIVEPADPSDATQLVASGKADFGVSYQESVLLARAKGlPVVSvaaLIQHPLSG-VISLKDSGIKSPKD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  149 LinlsqlvkqgKSKQYSIVYAGDTPSEYLALVldtKFDAFNLSDFRVIKVEDASQAWKLMQDtKENVAIAVL--WEPFvs 226
Cdd:pfam09084  91 L----------KGKRIGYSGSPFEEALLKALL---KKDGGDPDDVTIVNVGGMNLFPALLTG-KVDAAIGGYynWEGV-- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 498163171  227 QARKQGH-TVVLSSKD--APNTIVDVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:pfam09084 155 ELKLEGVeLNIFALADygVPDYYSLVLITNEAFLKENPELVRAFLRATLR 204
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
 218-357 3.49e-03

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 39.59  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 218 AVLWEPFVSQARKQGHTVVLSSK----DAPNtiVDVLVASDKVIQSQPEQISAFLAAYYRRIESGISNTSQLQDQIANDG 293
Cdd:PRK11480 173 AYVWAPAVNALEKDGKVLTDSEQvgqwGAPT--LDVWVVRKDFAEKHPEVVKAFAKSAIDAQQPYIANPDAWLKQPENIS 250

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 294 DLA------ASDADTVLKGINFFTALETQGWMQQeTLNERIRATAAVLVLSGNLTQVPDDPAQLYDPQFV 357
Cdd:PRK11480 251 KLArlsgvpEGDVPGLVKGNTYLTPQQQTAELTG-PVNKAIIDTAQFLKEQGKVPAVANDYSQYVTSRFV 319
 
Name Accession Description Interval E-value
OmpA_C-like cd07185
Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; ...
 413-514 4.07e-24

Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA; OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.


Pssm-ID: 143586 [Multi-domain]  Cd Length: 106  Bit Score: 96.85  E-value: 4.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 413 VKFAVGAADLTTTGRQTLDKLSKEIAEfNPDTvAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGK 491
Cdd:cd07185    4 IYFDFGSAELTPEAKPLLDKLAEVLKK-NPDA-KIRIEGHTDSRGSDAYNQELSERRAEAVADYLVSKGVDASrITAVGY 81

                         90       100
                 ....*....|....*....|....*
gi 498163171 492 GFSTPL-PGISPAD-ARNQRTEIRL 514
Cdd:cd07185   82 GESRPIaSNDTEEGrAKNRRVEIVI 106
OmpA COG2885
Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall ...
 274-516 5.32e-24

Outer membrane protein OmpA and related peptidoglycan-associated (lipo)proteins [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442131 [Multi-domain]  Cd Length: 294  Bit Score: 102.17  E-value: 5.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 274 RIESGISNTSQLQDQIANDGDLAASDADTVLKGINFFTALETQGWMQQETLNERIRATAAVLVLSGNLTQVPDDPAQLYD 353
Cdd:COG2885   50 SAGAAGGAAAGAEAGGLSAGLELLDAGSLSATAAAGAAALLVLLAALGALGAGLAALLLAIAAAASAAAADALALAAGAA 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 354 PQFVSQAAENTKKLIDIVRADNPELAQKLEGKTTAPTAAKPTADIKSAPSIGNLKVRGEVKFAVGAADLTTTGRQTLDKL 433
Cdd:COG2885  130 AALGALGASAAAAAAALAAAKALGDSAAAALDAAAKAEAAAAAAALLPAAVAEVVLLSNVYFDFDSAELTPEAKAALDEL 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 434 SKEIAEfNPDTVaVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGKGFSTPLPGISPADAR--NQRT 510
Cdd:COG2885  210 AALLKE-NPDLR-IEIEGHTDSRGSDAYNLALSERRAEAVKDYLVSKGIPASrITAVGYGESRPVASNDTEEGRakNRRV 287


                 ....*.
gi 498163171 511 EIRLVR 516
Cdd:COG2885  288 EIVVLK 293
PBP2_SsuA_like_6 cd13563
Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 ...
 94-273 3.53e-21

Putative substrate binding domain of sulfonate binding protein-like, a member of the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270281 [Multi-domain]  Cd Length: 208  Bit Score: 91.53  E-value: 3.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  94 QRAQALGQGKADFIVTTLDQFLKQKPKG---KIVGLIDRTVGADAVVLNtrqfPQLKSLINLsqlvkqgKSKQYSIVYAG 170
Cdd:cd13563   41 DSMAALASGQIDAAATTLDDALAMAAKGvpvKIVLVLDNSNGADGIVAK----PGIKSIADL-------KGKTVAVEEGS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 171 dtpSEYLALVLDTKFDAFNLSDFRVIKVE--DASQAWklmqdTKENVAIAVLWEPFVSQARKQGHTVVL-SSKDAPNTIV 247
Cdd:cd13563  110 ---VSHFLLLNALEKAGLTEKDVKIVNMTagDAGAAF-----IAGQVDAAVTWEPWLSNALKRGKGKVLvSSADTPGLIP 181

                        170       180
                 ....*....|....*....|....*.
gi 498163171 248 DVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:cd13563  182 DVLVVREDFIKKNPEAVKAVVKAWFD 207
OmpA pfam00691
OmpA family; The Pfam entry also includes MotB and related proteins which are not included in ...
 415-509 7.79e-17

OmpA family; The Pfam entry also includes MotB and related proteins which are not included in the Prosite family.


Pssm-ID: 425825 [Multi-domain]  Cd Length: 95  Bit Score: 75.86  E-value: 7.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  415 FAVGAADLTTTGRQTLDKLSKEIaEFNPDTVAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGI-KQTIQAEGKGF 493
Cdd:pfam00691   1 FDPGSSQLTPKAKATLDEIADLL-KFPELKNTITIEGHTDTVGSAAYNWELSQRRAEAVRRYLVNFGVpPSRISVVGYGA 79

                          90
                  ....*....|....*.
gi 498163171  494 STPLPGISPADARNQR 509
Cdd:pfam00691  80 TKPITDNKTPEGRARN 95
PRK10808 PRK10808
outer membrane protein A; Reviewed
 371-499 6.26e-15

outer membrane protein A; Reviewed


Pssm-ID: 236764 [Multi-domain]  Cd Length: 351  Bit Score: 76.27  E-value: 6.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 371 VRADNPELA--------QKLEGKTTAPTAA-KPTADIKSapsignLKVRGEVKFAVGAADLTTTGRQTLDKLSKEIAEFN 441
Cdd:PRK10808 181 ARPDNGMLSvgvsyrfgQEEAAPVVAPAPApAPVVQTKH------FTLKSDVLFNFNKATLKPEGQQALDQLYSQLSNLD 254

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498163171 442 PDTVAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGI-KQTIQAEGKGFSTPLPG 499
Cdd:PRK10808 255 PKDGSVVVLGYTDRIGSDAYNQGLSEKRAQSVVDYLVSKGIpADKISARGMGKSNPVTG 313
MotB COG1360
Flagellar motor protein MotB [Cell motility];
407-516 1.17e-13

Flagellar motor protein MotB [Cell motility];


Pssm-ID: 440971 [Multi-domain]  Cd Length: 174  Bit Score: 69.10  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 407 LKVRGEVKFAVGAADLTTTGRQTLDKLSKEIAEFNpdtVAVRVIGHTS----KTGSASLNQTLSQQRAQVVVQYLKQLGI 482
Cdd:COG1360   55 IEIQDRVLFDSGSAELTPEGRELLDKIAAVLAEVP---NRIRVEGHTDnvpiSTARFPSNWELSAARAAAVVRYLIEGGV 131

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 498163171 483 KQT-IQAEGKGFSTPL-PGISP-ADARNQRTEIRLVR 516
Cdd:COG1360  132 PPErLSAVGYGDTRPLaPNDTPeGRARNRRVEIVILR 168
TauA COG0715
ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion ...
 94-345 2.32e-13

ABC-type nitrate/sulfonate/bicarbonate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440479 [Multi-domain]  Cd Length: 297  Bit Score: 70.80  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  94 QRAQALGQGKADFIVTTLDQFLKQKPKG---KIVGLIDRTVGADAVVLNTRQFPQLKSLinlsqlvkQGKSkqysIVYAG 170
Cdd:COG0715   63 AALEALAAGQADFGVAGAPPALAARAKGapvKAVAALSQSGGNALVVRKDSGIKSLADL--------KGKK----VAVPG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 171 DTPSEY-LALVLDTkfDAFNLSDFRVIKVEDASQAWKLMQDtkeNVAIAVLWEPFVSQARKQG--HTVVLSSKDAPNTIV 247
Cdd:COG0715  131 GSTSHYlLRALLAK--AGLDPKDVEIVNLPPPDAVAALLAG---QVDAAVVWEPFESQAEKKGggRVLADSADLVPGYPG 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 248 DVLVASDKVIQSQPEQISAFLAAYYRRIESGISNTSQLQDQIANDGDLAASDADTVLKGinFFTALETQGWMQQetlnER 327
Cdd:COG0715  206 DVLVASEDFLEENPEAVKAFLRALLKAWAWAAANPDEAAAILAKATGLDPEVLAAALEG--DLRLDPPLGAPDP----AR 279

                        250
                 ....*....|....*...
gi 498163171 328 IRATAAVLVLSGNLTQVP 345
Cdd:COG0715  280 LQRVADFLVELGLLPKDV 297
PRK09039 PRK09039
peptidoglycan -binding protein;
412-514 2.77e-11

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 64.99  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 412 EVKFAVGAADLTTTGRQTLDKLS---KEIAEFNPDTVA--VRVIGHT-----SKTGSASLNQTLSQQRAQVVVQYLKQLG 481
Cdd:PRK09039 225 EVLFPTGSAELNPEGQAEIAKLAaalIELAKEIPPEINwvLRVDGHTdnvplSGTGRFRDNWELSSARAISVVKFLIALG 304

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 498163171 482 I-KQTIQAEGKGFSTPL-PGISPAD-ARNQRTEIRL 514
Cdd:PRK09039 305 VpADRLAAAGFGEFQPLdPGDTPEArARNRRIELKL 340
PRK10510 PRK10510
OmpA family lipoprotein;
413-514 2.90e-10

OmpA family lipoprotein;


Pssm-ID: 182507 [Multi-domain]  Cd Length: 219  Bit Score: 60.27  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 413 VKFAVGAADLTTTGRQTLDKLSKEIAEFnpDTVAVRVIGHTSKTGSASLNQTLSQQRAQVVVQYLKQLGIKQT-IQAEGK 491
Cdd:PRK10510 114 VTFDSSSATLKPAGANTLTGVAMVLKEY--PKTAVNVVGYTDSTGSHDLNMRLSQQRADSVASALITQGVDASrIRTQGM 191

                         90       100
                 ....*....|....*....|....*
gi 498163171 492 GFSTPLPGISPAD--ARNQRTEIRL 514
Cdd:PRK10510 192 GPANPIASNSTAEgkAQNRRVEITL 216
PBP2_SsuA_like_5 cd13562
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
 156-273 2.11e-08

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes sulfonate binding domains found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270280 [Multi-domain]  Cd Length: 215  Bit Score: 54.82  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 156 VKQGKSKQYSIVYaGDTPSEYLALVLDTKfdAFNLSDFRVIKVEDASQAWKLmqdTKENVAIAVLWEPFVSQARKQGHTV 235
Cdd:cd13562  103 VKDLKGKKVATTK-GSYVHHLLVLVLQEA--GLTIDDVEFINMQQADMNTAL---TNGDIDAAVIWEPLITKLLSDGVVR 176

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 498163171 236 VLSSKDAPNTIVDVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:cd13562  177 VLRDGTGIKDGLNVIVARGPLIEQNPEVVKALLKAYQR 214
PRK07033 PRK07033
DotU family type VI secretion system protein;
409-514 2.82e-07

DotU family type VI secretion system protein;


Pssm-ID: 180801 [Multi-domain]  Cd Length: 427  Bit Score: 52.74  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 409 VRGEVKFAVGAADLTTTGRQTLDKLSKEIAEFNPDtvaVRVIGHTSKTGSASL----NQTLSQQRAQVVVQYL-KQLGIK 483
Cdd:PRK07033 312 LRGDGLFASASTSVRDRYQPVLARVADALNQVKGN---VLVTGYSDNVPIRTArfpsNWELSQARAQAVRALLaARLGQP 388

                         90       100       110
                 ....*....|....*....|....*....|...
gi 498163171 484 QTIQAEGKGFSTPL-PGISPAD-ARNQRTEIRL 514
Cdd:PRK07033 389 ERVTAEGRGDSDPVaPNDSAENrARNRRVEITL 421
PRK08126 PRK08126
hypothetical protein; Provisional
 410-516 3.96e-07

hypothetical protein; Provisional


Pssm-ID: 236157 [Multi-domain]  Cd Length: 432  Bit Score: 52.39  E-value: 3.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 410 RGEVKFAVGAADLTTTGRQTLDKLSKEIAEFNPdtvAVRVIGHTS----KTGSASLNQTLSQQRAQVVVQYLKQLGIKQT 485
Cdd:PRK08126 322 RGDAMFVPGQATVNPAMGPLIAKIAREIARVGG---KVTVTGHTDnqpiRSAQFASNLVLSEKRAAQVAQMLQSAGVPAS 398

                         90       100       110
                 ....*....|....*....|....*....|....
gi 498163171 486 -IQAEGKGFSTPLPGISPAD--ARNQRTEIRLVR 516
Cdd:PRK08126 399 rLEAVGKGDAQPVADNRTPQgrAQNRRVEITVAE 432
PBP2_ThiY_THI5_like_1 cd13652
Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 ...
 214-271 9.86e-06

Putative substrate binding domain of an ABC-type transporter similar to ThiY/THI5; the type 2 periplasmic binding protein fold; This subfamily is phylogenetically similar to ThiY, which is the periplasmic N-formyl-4-amino-5-(aminomethyl)-2-methylpyrimidine (FAMP) binding component of the ABC transport system (ThiXYZ). FAMP is imported into cell by the transporter, where it is then incorporated into the thiamin biosynthetic pathway. The closest structural homologs of ThiY are THI5, which is responsible for the synthesis of 4-amino-5-(hydroxymethyl)-2-methylpyrimidine phosphate (HMP-P) in the thiamin biosynthetic pathway of eukaryotes, and periplasmic binding proteins involved in alkanesulfonate/nitrate and bicarbonate transport. After binding the ligand, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ThiY/THI5 proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270370 [Multi-domain]  Cd Length: 217  Bit Score: 46.61  E-value: 9.86e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 498163171 214 NVAIAVLWEPFVSQARKQGHTVVLSSKDAP-NTIVDVLVASDKVIQSQPEQISAFLAAY 271
Cdd:cd13652  156 NVDAAVLAEPFLSRARSSGAKVVASDYADPdPHSQATMVFSADFARENPEVVKKFLRAY 214
PBP2_NrtA_SsuA_CpmA_like cd01008
Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of ...
 97-273 3.87e-05

Substrate binding domain of ABC-type nitrate/sulfonate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This family represents the periplasmic binding proteins involved in nitrate, alkanesulfonate, and bicarbonate transport. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates. Other closest homologs involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB) are also included in this family. After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270229 [Multi-domain]  Cd Length: 212  Bit Score: 44.97  E-value: 3.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  97 QALGQGKADFIV---TTLDQFLKQKPKGKIVGLIDRTVGADAVVLntRQFPQLKSLINLsqlvkQGKSkqysIVYAGDTP 173
Cdd:cd01008   46 EALAAGSLDFGTggdTPALLAAAGGVPVVLIAALSRSPNGNGIVV--RKDSGITSLADL-----KGKK----IAVTKGTT 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 174 SEYLALvldTKFDAFNLS--DFRVIKV--EDASQAWKlmqdtKENVAIAVLWEPFVSQARKQGHT-VVLSSKDAPNTIVD 248
Cdd:cd01008  115 GHFLLL---KALAKAGLSvdDVELVNLgpADAAAALA-----SGDVDAWVTWEPFLSLAEKGGDArIIVDGGGLPYTDPS 186

                        170       180
                 ....*....|....*....|....*
gi 498163171 249 VLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:cd01008  187 VLVARRDFVEENPEAVKALLKALVE 211
PBP2_NrtA_CpmA_like cd13553
Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 ...
 218-271 7.68e-05

Substrate binding domain of ABC-type nitrate/bicarbonate transporters, a member of the type 2 periplasmic binding fold superfamily; This subfamily includes nitrate (NrtA) and bicarbonate (CmpA) receptors. These domains are found in eubacterial perisplamic-binding proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding their ligand with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. These binding proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270271 [Multi-domain]  Cd Length: 212  Bit Score: 44.11  E-value: 7.68e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 498163171 218 AVLWEPFVSQARKQ--GHTVVLSSKDAPNTIVDVLVASDKVIQSQPEQISAFLAAY 271
Cdd:cd13553  154 YCVGEPWNARAVAEgvGRVLADSGDIWPGHPCCVLVVREDFLEENPEAVQALLKAL 209
NMT1 pfam09084
NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed ...
 73-273 8.04e-05

NMT1/THI5 like; This family contains the NMT1 and THI5 proteins. These proteins are proposed to be required for the biosynthesis of the pyrimidine moiety of thiamine.3]. They are regulated by thiamine. The protein adopts a fold related to the periplasmic binding protein (PBP) family. Both pyridoxal-5'-phosphate (PLP) and an iron atom are bound to the protein suggesting numerous residues of the active site necessary for HMP-P biosynthesis. The yeast protein is a dimer and, although exceptionally using PLP as a substrate, has notable similarities with enzymes dependent on this molecule as a cofactor.


Pssm-ID: 430398 [Multi-domain]  Cd Length: 216  Bit Score: 44.13  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171   73 FQEAlgepGIRLDYADEFDQFQRAQALGQGKADFIVTTLDQFLKQKPKG-KIVG---LIDRTVGAdAVVLNTRQFPQLKS 148
Cdd:pfam09084  16 FKEE----GLDVEIVEPADPSDATQLVASGKADFGVSYQESVLLARAKGlPVVSvaaLIQHPLSG-VISLKDSGIKSPKD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171  149 LinlsqlvkqgKSKQYSIVYAGDTPSEYLALVldtKFDAFNLSDFRVIKVEDASQAWKLMQDtKENVAIAVL--WEPFvs 226
Cdd:pfam09084  91 L----------KGKRIGYSGSPFEEALLKALL---KKDGGDPDDVTIVNVGGMNLFPALLTG-KVDAAIGGYynWEGV-- 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 498163171  227 QARKQGH-TVVLSSKD--APNTIVDVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:pfam09084 155 ELKLEGVeLNIFALADygVPDYYSLVLITNEAFLKENPELVRAFLRATLR 204
tauA PRK11480
taurine transporter substrate binding subunit; Provisional
 218-357 3.49e-03

taurine transporter substrate binding subunit; Provisional


Pssm-ID: 183158  Cd Length: 320  Bit Score: 39.59  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 218 AVLWEPFVSQARKQGHTVVLSSK----DAPNtiVDVLVASDKVIQSQPEQISAFLAAYYRRIESGISNTSQLQDQIANDG 293
Cdd:PRK11480 173 AYVWAPAVNALEKDGKVLTDSEQvgqwGAPT--LDVWVVRKDFAEKHPEVVKAFAKSAIDAQQPYIANPDAWLKQPENIS 250

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498163171 294 DLA------ASDADTVLKGINFFTALETQGWMQQeTLNERIRATAAVLVLSGNLTQVPDDPAQLYDPQFV 357
Cdd:PRK11480 251 KLArlsgvpEGDVPGLVKGNTYLTPQQQTAELTG-PVNKAIIDTAQFLKEQGKVPAVANDYSQYVTSRFV 319
PBP2_SsuA_like_4 cd13561
Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic ...
 215-273 8.77e-03

Putative substrate binding domain of sulfonate binding protein-like, the type 2 periplasmic binding protein fold; This subfamily includes the periplasmic component of putative ABC-type sulfonate transport system similar to SsuA. These domains are found in eubacterial SsuA proteins that serve as initial receptors in the ABC transport of bicarbonate, nitrate, taurine, or a wide range of aliphatic sulfonates, while other closest homologs are involved in thiamine (vitamin B1) biosynthetic pathway and desulfurization (DszB). After binding the ligand, SsuA interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The SsuA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270279 [Multi-domain]  Cd Length: 212  Bit Score: 37.74  E-value: 8.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498163171 215 VAIAVLWEPFVSQARKQGHTVV--LSSKD--APNTIVDVLVASDKVIQSQPEQISAFLAAYYR 273
Cdd:cd13561  149 VDAAALWAPNTATIKEKVPGAVelADNSDfgPDAAVPGAWVARNKYAEENPEELKKFLAALAE 211
 
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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