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Conserved domains on  [gi|447201370|ref|WP_001278626|]
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MULTISPECIES: HlyD family secretion protein [Acinetobacter]

Protein Classification

HlyD family secretion protein( domain architecture ID 11446287)

HlyD family secretion protein similar to Escherichia coli protein YhiI, Acinetobacter baumannii colistin resistance protein EmrA, and Burkholderia cepacia fusaric acid resistance protein FusE

Gene Ontology:  GO:0022857|GO:0016020|GO:0055085
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
36-373 1.47e-82

Multidrug resistance efflux pump EmrA [Defense mechanisms];


:

Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 254.97  E-value: 1.47e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWAWRIGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:COG1566    2 KALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQkQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG1566   82 QAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 196 LAALKQAEANVLVAKEALKT-AQVAEAglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYL 274
Cdd:COG1566  161 QAQLEAAQAQLAQAQAGLREeEELAAA--QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 275 IP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPAAGSEFSvlkPDNATGNftkVVQRIAVRITIDP 353
Cdd:COG1566  239 VPlDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSP---PKNATGN---VVQRYPVRIRLDN 312
                        330       340
                 ....*....|....*....|
gi 447201370 354 NQEgmEHLRPGMSVITSVDT 373
Cdd:COG1566  313 PDP--EPLRPGMSATVEIDT 330
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
36-373 1.47e-82

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 254.97  E-value: 1.47e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWAWRIGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:COG1566    2 KALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQkQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG1566   82 QAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 196 LAALKQAEANVLVAKEALKT-AQVAEAglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYL 274
Cdd:COG1566  161 QAQLEAAQAQLAQAQAGLREeEELAAA--QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 275 IP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPAAGSEFSvlkPDNATGNftkVVQRIAVRITIDP 353
Cdd:COG1566  239 VPlDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSP---PKNATGN---VVQRYPVRIRLDN 312
                        330       340
                 ....*....|....*....|
gi 447201370 354 NQEgmEHLRPGMSVITSVDT 373
Cdd:COG1566  313 PDP--EPLRPGMSATVEIDT 330
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
36-375 2.52e-49

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 170.65  E-value: 2.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWaWRIgpFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:PRK15136  21 KRALLLLTLLFIIIGVAYGIY-WFL--VLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQkvaqaasGVEQAKNTLANQTQSIAQKQADIVAAQAKVEqVRaQYELSLAQ--LRRYQQLGNSGAASKsEQDKAAADAe 193
Cdd:PRK15136  98 EQ-------AFEKAKTALANSVRQTHQLMINSKQYQANIE-LQ-KTALAQAQsdLNRRVPLGNANLIGR-EELQHARDA- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 194 nnlAALKQAEANVLVAKEALKTAQVAEAGLEAQ--VSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQL 271
Cdd:PRK15136 167 ---VASAQAQLDVAIQQYNANQAMILNTPLEDQpaVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 272 LYLIP-QQTWVIANFKETQIANMRIGQKAWFTVDAM-KHKKFTGHVEQISPAAGSEFSVLKPDNATGNFTKVVQRIAVRI 349
Cdd:PRK15136 244 MAVVPaTNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRI 323
                        330       340
                 ....*....|....*....|....*.
gi 447201370 350 TIDPNQEGMEHLRPGMSVITSVDTSS 375
Cdd:PRK15136 324 ELDAKQLAQHPLRIGLSTLVTVDTAN 349
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
60-366 6.46e-35

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 130.62  E-value: 6.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370   60 IGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQA----------------- 122
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAeaqlakaqaqvarlqae 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  123 ASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS---EQDKAAADAENNLAAL 199
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISREslvTAGALVAQAQANLLAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  200 KQAEANVLVAKEALKTAQVAEA-----GLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRV-GQYVAAGSQLLY 273
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVrselsGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  274 LIP-QQTWVIANFKETQIANMRIGQKAWFTVDAM---KHKKFTGHVEQISPAAGSefsvlkpdnatgnftkvvqriaVRI 349
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFpqtKTGRFTGVVVGISPDTGP----------------------VRV 298
                         330
                  ....*....|....*..
gi 447201370  350 TIDPNQEGMEHLRPGMS 366
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLS 315
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
77-367 3.51e-24

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 101.24  E-value: 3.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370   77 GKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYdqkvaqaasgveqakntlanqtqsiaqkQADIVAAQAKVEQ 156
Cdd:TIGR01730  24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDY----------------------------QLALQAALAQLAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  157 VRAQYELSLAQLRRYQQLGNSGAASKSEQDKaaadaennlaalkqaeanvlvakealktAQVAEAGLEAQVSSAKAQLDQ 236
Cdd:TIGR01730  76 AEAQLELAQRSFERAERLVKRNAVSQADLDD----------------------------AKAAVEAAQADLEAAKASLAS 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  237 AQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHV 315
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDlDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 447201370  316 EQISPAAgsefsvlkpDNATGNFtkvvqriAVRITIDPNQEGmehLRPGMSV 367
Cdd:TIGR01730 208 RFIDPRV---------DSGTGTV-------RVRATFPNPDGR---LLPGMFG 240
 
Name Accession Description Interval E-value
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
36-373 1.47e-82

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 254.97  E-value: 1.47e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWAWRIGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:COG1566    2 KALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQkQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG1566   82 QAALAQAEAQLAAAEAQLARLEAELGA-EAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 196 LAALKQAEANVLVAKEALKT-AQVAEAglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYL 274
Cdd:COG1566  161 QAQLEAAQAQLAQAQAGLREeEELAAA--QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 275 IP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPAAGSEFSvlkPDNATGNftkVVQRIAVRITIDP 353
Cdd:COG1566  239 VPlDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSP---PKNATGN---VVQRYPVRIRLDN 312
                        330       340
                 ....*....|....*....|
gi 447201370 354 NQEgmEHLRPGMSVITSVDT 373
Cdd:COG1566  313 PDP--EPLRPGMSATVEIDT 330
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
36-375 2.52e-49

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 170.65  E-value: 2.52e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWaWRIgpFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTY 115
Cdd:PRK15136  21 KRALLLLTLLFIIIGVAYGIY-WFL--VLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQkvaqaasGVEQAKNTLANQTQSIAQKQADIVAAQAKVEqVRaQYELSLAQ--LRRYQQLGNSGAASKsEQDKAAADAe 193
Cdd:PRK15136  98 EQ-------AFEKAKTALANSVRQTHQLMINSKQYQANIE-LQ-KTALAQAQsdLNRRVPLGNANLIGR-EELQHARDA- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 194 nnlAALKQAEANVLVAKEALKTAQVAEAGLEAQ--VSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQL 271
Cdd:PRK15136 167 ---VASAQAQLDVAIQQYNANQAMILNTPLEDQpaVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 272 LYLIP-QQTWVIANFKETQIANMRIGQKAWFTVDAM-KHKKFTGHVEQISPAAGSEFSVLKPDNATGNFTKVVQRIAVRI 349
Cdd:PRK15136 244 MAVVPaTNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRI 323
                        330       340
                 ....*....|....*....|....*.
gi 447201370 350 TIDPNQEGMEHLRPGMSVITSVDTSS 375
Cdd:PRK15136 324 ELDAKQLAQHPLRIGLSTLVTVDTAN 349
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
78-375 1.84e-43

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 153.18  E-value: 1.84e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  78 KTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYdqkvaqaasgveqakntlanqtqsiaqkQADIVAAQAKVEQV 157
Cdd:COG0845   22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDL----------------------------QAALAQAQAQLAAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 158 RAQYELSLAQLRRYQQLGNSGAASKSEqdkaaadaennlaaLKQAEANVLVAkealktaqvaeaglEAQVSSAKAQLDQA 237
Cdd:COG0845   74 QAQLELAKAELERYKALLKKGAVSQQE--------------LDQAKAALDQA--------------QAALAAAQAALEQA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 238 QTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLI-PQQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVE 316
Cdd:COG0845  126 RANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIAdLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVT 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 447201370 317 QISPAAgsefsvlkpDNATGNFTkvvqriaVRITIdPNQEGMehLRPGMSVITSVDTSS 375
Cdd:COG0845  206 FIDPAV---------DPATRTVR-------VRAEL-PNPDGL--LRPGMFVRVRIVLGE 245
PRK10476 PRK10476
multidrug transporter subunit MdtN;
34-358 6.21e-38

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 139.39  E-value: 6.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  34 PTKRSTLLWMLGVLIIGILVILwAWRIGPFATsvqqTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDAT 113
Cdd:PRK10476   8 SPRKKLPALAIVALAIVALVFV-IWRTDSAPS----TDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 114 TYDQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAA--- 190
Cdd:PRK10476  83 PYELTVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTaqr 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 191 DAENNL-AALKQAEANVlvakealkTAQVAEAGLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGS 269
Cdd:PRK10476 163 DAEVSLnQALLQAQAAA--------AAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 270 QLLYLIPQQTW-VIANFKETQIANMRIGQKAwfTVDAM--KHKKFTGHVEQISPAAGSEFSVLKPDN-----ATGNFTKV 341
Cdd:PRK10476 235 PIFTLIDTDHWyAIANFRETDLKNIRVGDCA--TVYSMidRGRPFEGKVDSIGWGVLPDDGGNVPRGlpyvpRSINWVRV 312
                        330
                 ....*....|....*...
gi 447201370 342 VQRIAVRITID-PNQEGM 358
Cdd:PRK10476 313 AQRFPVRIMLDkPDPELF 330
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
60-366 6.46e-35

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 130.62  E-value: 6.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370   60 IGPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQA----------------- 122
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAeaqlakaqaqvarlqae 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  123 ASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS---EQDKAAADAENNLAAL 199
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISREslvTAGALVAQAQANLLAT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  200 KQAEANVLVAKEALKTAQVAEA-----GLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRV-GQYVAAGSQLLY 273
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEVrselsGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  274 LIP-QQTWVIANFKETQIANMRIGQKAWFTVDAM---KHKKFTGHVEQISPAAGSefsvlkpdnatgnftkvvqriaVRI 349
Cdd:pfam00529 241 VVPeDNLLVPGMFVETQLDQVRVGQPVLIPFDAFpqtKTGRFTGVVVGISPDTGP----------------------VRV 298
                         330
                  ....*....|....*..
gi 447201370  350 TIDPNQEGMEHLRPGMS 366
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLS 315
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
36-374 2.66e-24

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 101.96  E-value: 2.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWAWRIgpfatsvQQTDNSY-----VKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHI 110
Cdd:PRK03598   2 KKKVVIGLAVVVLAAAVAGGWWWYQ-------SRQDNGLtlygnVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 111 DATTYDQKVAQAASGVEQAKNTLA-----NQTQSIAQkqadivaAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASkseq 185
Cdd:PRK03598  75 DAAPYENALMQAKANVSVAQAQLDlmlagYRDEEIAQ-------ARAAVKQAQAAYDYAQNFYNRQQGLWKSRTIS---- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 186 dkaAADAENNLAALKQAEANVLVAKEALKTAQ-------VAEAglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVN 258
Cdd:PRK03598 144 ---ANDLENARSSRDQAQATLKSAQDKLSQYRegnrpqdIAQA--KASLAQAQAALAQAELNLQDTELIAPSDGTILTRA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 259 PRVGQYVAAGSQLLYL-IPQQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPAAgsEF---SVLKPDNA 334
Cdd:PRK03598 219 VEPGTMLNAGSTVFTLsLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTA--EFtpkTVETPDLR 296
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 447201370 335 tgnfTKVVQRIavRITIDPNQEGmehLRPGMSVITSVDTS 374
Cdd:PRK03598 297 ----TDLVYRL--RIVVTDADDA---LRQGMPVTVRFADE 327
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
77-367 3.51e-24

RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 273776 [Multi-domain]  Cd Length: 322  Bit Score: 101.24  E-value: 3.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370   77 GKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYdqkvaqaasgveqakntlanqtqsiaqkQADIVAAQAKVEQ 156
Cdd:TIGR01730  24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDY----------------------------QLALQAALAQLAA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  157 VRAQYELSLAQLRRYQQLGNSGAASKSEQDKaaadaennlaalkqaeanvlvakealktAQVAEAGLEAQVSSAKAQLDQ 236
Cdd:TIGR01730  76 AEAQLELAQRSFERAERLVKRNAVSQADLDD----------------------------AKAAVEAAQADLEAAKASLAS 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  237 AQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIP-QQTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHV 315
Cdd:TIGR01730 128 AQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDlDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 447201370  316 EQISPAAgsefsvlkpDNATGNFtkvvqriAVRITIDPNQEGmehLRPGMSV 367
Cdd:TIGR01730 208 RFIDPRV---------DSGTGTV-------RVRATFPNPDGR---LLPGMFG 240
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
36-320 2.09e-21

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 94.07  E-value: 2.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  36 KRSTLLWMLGVLIIGILVILWAWRIGPFAT----SVQQTD---NSYVKGKTTIL-----SSQINGYVKDVLVKDFDHVKK 103
Cdd:PRK11578   6 KVKKRYLIALVIVLAGGITLWRILNAPVPTyqtlIVRPGDlqqSVLATGKLDALrkvdvGAQVSGQLKTLSVAIGDKVKK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 104 GQVLMHIDAttydqkvaqaasgvEQAKNtlanqtqSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS 183
Cdd:PRK11578  86 DQLLGVIDP--------------EQAEN-------QIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 184 EQDKAAADAennlaalkqaeanvlvakeALKTAQVAEagLEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQ 263
Cdd:PRK11578 145 DLDTAATEL-------------------AVKQAQIGT--IDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQ 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447201370 264 YVAAGSQ---LLYLIPQQTW-VIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISP 320
Cdd:PRK11578 204 TVIAAQQapnILTLADMSTMlVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILP 264
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
78-367 2.93e-15

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 74.08  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370   78 KTTILSSQINGYVKDVLVKDF-DHVKKGQVLMHIDATtydqkvaqaasgveqakntlanqtqsiaqkqaDIVAAQAkveq 156
Cdd:pfam16576  18 RLAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYSP--------------------------------ELVAAQQ---- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  157 vraqyELSLAQlrryqqlgNSGAASKSEQDKAAAdaennlaalkqaeanvlvaKEALKTAQVAEAGLeaqvssakAQLDQ 236
Cdd:pfam16576  62 -----EYLLAL--------RSGDALSKSELLRAA-------------------RQRLRLLGMPEAQI--------AELER 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  237 AQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGsQLLYLIPQ--QTWVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGH 314
Cdd:pfam16576 102 TGKVQPTVTVYAPISGVVTELNVREGMYVQPG-DTLFTIADlsTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGK 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 447201370  315 VEQISPaagsefsVLKPDNATgnftkvvqrIAVRITIdPNQEGMehLRPGMSV 367
Cdd:pfam16576 181 VDYIYP-------TLDPKTRT---------VRVRIEL-PNPDGR--LKPGMFA 214
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
31-373 4.20e-13

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 69.38  E-value: 4.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  31 KLIPTKRSTLLWMLGVLIIGILVILWAWrigPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHI 110
Cdd:PRK10559   2 KTLIRKISRTAITLVLVILAFIAIFRAW---VFYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 111 DATTYDQKVAQAasgveqakntlanqtqsiaqkQADIVAAQAKVEQVRAQYElslaqlrRYQQLGNSgAASKSEQDKAaa 190
Cdd:PRK10559  79 DQPRYQKALAEA---------------------EADVAYYQVLAQEKRREAG-------RRNRLGVQ-AMSREEIDQA-- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 191 daeNNlaalkqaeanvlvakeALKTAqvaeaglEAQVSSAKAQLDQAQTTKDYSVIVAPMDGQLGEVNPRVGQYVAAGSQ 270
Cdd:PRK10559 128 ---NN----------------VLQTV-------LHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGST 181
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 271 LLYLIPQQT-WVIANFKETQIANMRIGQKAWFTvDAMKHKKFTGHVEQIspAAGSEFSVLKPDN---ATGN----FTKVV 342
Cdd:PRK10559 182 AVALVKQNSfYVLAYMEETKLEGVRPGYRAEIT-PLGSNKVLKGTVDSV--AAGVTNSSSTRDSkgmATIDsnleWVRLA 258
                        330       340       350
                 ....*....|....*....|....*....|.
gi 447201370 343 QRIAVRITIDPNQegmEHLRPGMSVITSVDT 373
Cdd:PRK10559 259 QRVPVRIRLDNQQ---GNLYPAGTTATVVIT 286
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
46-375 6.08e-13

type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 130902 [Multi-domain]  Cd Length: 423  Bit Score: 69.65  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370   46 VLIIGILVILWAWRI-GPFATSVQQTDNSYVKGKTTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATT---------- 114
Cdd:TIGR01843   9 WLIAGLVVIFFLWAYfAPLDVVATATGKVVPSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDveadaaeles 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  115 -----------------------------------YDQKVAQAASGVEQAKNTLANQTQSI----AQKQADIVAAQAKVE 155
Cdd:TIGR01843  89 qvlrleaevarlraeadsqaaiefpddllsaedpaVPELIKGQQSLFESRKSTLRAQLELIlaqiKQLEAELAGLQAQLQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  156 QVRAQYELSLAQLRRYQQLGNSGAASKS---EQDKAAADAENNLAALKqAEANVLVAK--------------------EA 212
Cdd:TIGR01843 169 ALRQQLEVISEELEARRKLKEKGLVSRLellELERERAEAQGELGRLE-AELEVLKRQidelqlerqqieqtfreevlEE 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  213 LKTAQVAEAGLEAQVSSAKAQLDQaqttkdySVIVAPMDGQLGEV-NPRVGQYVAAGSQLLYLIP--QQTWVIANFKETQ 289
Cdd:TIGR01843 248 LTEAQARLAELRERLNKARDRLQR-------LIIRSPVDGTVQSLkVHTVGGVVQPGETLMEIVPedDPLEIEAKLSPKD 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  290 IANMRIGQKAWFTVDAMKHKKF---TGHVEQISPAAGSEfsvlkpDNATGNFTKVvqriavRITIDPNQEGME----HLR 362
Cdd:TIGR01843 321 IGFVHVGQPAEIKFSAFPYRRYgilNGKVKSISPDTFTD------ERGGGPYYRV------RISIDQNTLGIGpkglELS 388
                         410
                  ....*....|...
gi 447201370  363 PGMSVITSVDTSS 375
Cdd:TIGR01843 389 PGMPVTADIKTGE 401
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
245-364 8.70e-11

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 58.53  E-value: 8.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  245 VIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIPQQT-WVIANFKETQIANMRIGQKAWFTVDAMKHKKFTGHVEQISPaag 323
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRlLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISP--- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 447201370  324 sefsvlKPDNATGNFTkvvqriaVRITIDPNQEGmEHLRPG 364
Cdd:pfam13437  78 ------TVDPDTGVIP-------VRVSIENPKTP-IPLLPG 104
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
64-299 2.79e-09

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 58.26  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  64 ATSVQQTDNSYVKGKTTI-------LSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQAASGVEQAKNTLANQ 136
Cdd:PRK11556  65 ATATEQAVPRYLTGLGTVtaantvtVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 137 TQSIAqkqadivaaqakveqvraqyelslaqlrRYQQLGNSGAASKSEQDkaaadaeNNLAALKQAEANVLVAkealkta 216
Cdd:PRK11556 145 RRDLA----------------------------RYQQLAKTNLVSRQELD-------AQQALVSETEGTIKAD------- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 217 qvaeaglEAQVSSAKAQLDqaqttkdYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIPQQTW---VIANFKETQIANM 293
Cdd:PRK11556 183 -------EASVASAQLQLD-------YSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHpidLVFTLPESDIATV 248

                 ....*.
gi 447201370 294 RIGQKA 299
Cdd:PRK11556 249 VQAQKA 254
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
116-242 1.54e-07

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQyeLSLAQLRRyQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG1196  259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD--IARLEERR-RELEERLEELEEELAELEEELEEL 335
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 447201370 196 LAALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:COG1196  336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
TolC COG1538
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
119-215 2.63e-06

Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441147 [Multi-domain]  Cd Length: 367  Bit Score: 48.88  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 119 VAQAASGVEQAKNTLANQTQSIAQ--KQA--DIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAEN 194
Cdd:COG1538   53 IEAAKAQAEAAEADLRAARLDLAAevAQAyfDLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQ 132
                         90       100
                 ....*....|....*....|.
gi 447201370 195 NLAALKQAEANVLVAKEALKT 215
Cdd:COG1538  133 ARAQLAQAEAQLAQARNALAL 153
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
116-233 8.40e-06

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.56  E-value: 8.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIvAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG2268  222 EAEEAELEQEREIETARIAEAEAELAKKKAEE-RREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAE 300
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 447201370 196 LAaLKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQ 233
Cdd:COG2268  301 RE-EAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGL 337
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
133-242 1.54e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  133 LANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKS-----------EQDKAAADAENN-LAALK 200
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaelEAELERLDASSDdLAALE 691
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 447201370  201 Q----AEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:COG4913   692 EqleeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
79-122 2.08e-05

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 41.27  E-value: 2.08e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 447201370   79 TTILSSQINGYVKDVLVKDFDHVKKGQVLMHIDATTYDQKVAQA 122
Cdd:pfam13533   2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQA 45
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
187-252 2.26e-05

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 45.94  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 187 KAAADAENnlAALKQAEANVLVAKEALK-----------------TAQVAEAGLEAQVSSAKAQLDQAQTTKDYSVIVAP 249
Cdd:PRK09578 100 KAARDAAA--GALAKAEAAHLAALDKRRryddlvrdravserdytEAVADERQAKAAVASAKAELARAQLQLDYATVTAP 177

                 ...
gi 447201370 250 MDG 252
Cdd:PRK09578 178 IDG 180
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
111-235 3.07e-05

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 45.49  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  111 DATTYDQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQyelsLAQLrryqqlgnsgaaskseQDKAAA 190
Cdd:TIGR04320 255 SLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKE----LANA----------------QAQALQ 314
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 447201370  191 DAENNLAALKQAEANvlvAKEALKTAQVAEAGLEAQVSSAKAQLD 235
Cdd:TIGR04320 315 TAQNNLATAQAALAN---AEARLAKAKEALANLNADLAKKQAALD 356
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
152-339 3.21e-05

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 45.48  E-value: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 152 AKVEQVRAQYELSLAQL--RRYQQLGNSGAASKSEQDKAAADAEnnlaalkQAEANVLVAKEALKTAQVAEAgleaqvss 229
Cdd:PRK15030 108 AKGDLAKAQAAANIAQLtvNRYQKLLGTQYISKQEYDQALADAQ-------QANAAVTAAKAAVETARINLA-------- 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 230 akaqldqaqttkdYSVIVAPMDGQLGEVNPRVGQYVAAGSQLLYLIPQQTWVIAnFKETQIANMRIGQKAWFTVDAMKHK 309
Cdd:PRK15030 173 -------------YTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIY-VDVTQSSNDFLRLKQELANGTLKQE 238
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 447201370 310 KFTGHVEQIS------PAAGS-EFSVLKPDNATGNFT 339
Cdd:PRK15030 239 NGKAKVSLITsdgikfPQDGTlEFSDVTVDQTTGSIT 275
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
129-242 8.61e-05

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 43.95  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  129 AKNTLANQTQSIAQKQADIVAAQAKVEQvrAQYELSLAQlrryQQLGNSGAASKSEQdKAAADAENNLA-----ALKQAE 203
Cdd:TIGR04320 245 DKTPIPNPPNSLAALQAKLATAQADLAA--AQTALNTAQ----AALTSAQTAYAAAQ-AALATAQKELAnaqaqALQTAQ 317
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 447201370  204 ANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:TIGR04320 318 NNLATAQAALANAEARLAKAKEALANLNADLAKKQAALD 356
PRK12472 PRK12472
hypothetical protein; Provisional
112-274 5.33e-04

hypothetical protein; Provisional


Pssm-ID: 237110 [Multi-domain]  Cd Length: 508  Bit Score: 41.78  E-value: 5.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 112 ATTYDQKVAQAASGVEQAKNTLAnqtqSIAQKQADIVAAQAKVEQVRAQYElslAQLRRYQQlgnSGAASKSEQDKAAAD 191
Cdd:PRK12472 192 AETLAREAEDAARAADEAKTAAA----AAAREAAPLKASLRKLERAKARAD---AELKRADK---ALAAAKTDEAKARAE 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 192 AENNLAALKQAEANvlvakEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKDYSVIVApMDGQLGeVNPrVGQYVAAGSQL 271
Cdd:PRK12472 262 ERQQKAAQQAAEAA-----TQLDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAA-TDAKLA-LEP-VSIYISRATQK 333

                 ...
gi 447201370 272 LYL 274
Cdd:PRK12472 334 LYV 336
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
116-254 8.48e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQyeLSLAQ-LRRYQQLGNSGAASKSEQDKAAADAEN 194
Cdd:COG1579   37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--LGNVRnNKEYEALQKEIESLKRRISDLEDEILE 114
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447201370 195 NLAALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQ--AQTTKDYSVIVAPMDGQL 254
Cdd:COG1579  115 LMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAelEELEAEREELAAKIPPEL 176
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
116-241 2.06e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 116 DQKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYElslAQLRRYQQLGNSGAASKSEQDKAAADAENN 195
Cdd:COG4942   61 ERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA---ELLRALYRLGRQPPLALLLSPEDFLDAVRR 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447201370 196 LAALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTK 241
Cdd:COG4942  138 LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
117-242 2.48e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.14  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 117 QKVAQAASGVEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRaqyelslAQLRRYQQLGNSGAASKsEQDKAAADAENNL 196
Cdd:COG1579   31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE-------ARIKKYEEQLGNVRNNK-EYEALQKEIESLK 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 447201370 197 AALKQAEANVLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQTTKD 242
Cdd:COG1579  103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
145-242 2.75e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370  145 ADIVAAQAKVEQVRAQYELsLAQLRRYQQlgnsgAASKSEQDKAAADAENNLAALKQAEANVLVAKEALKTAQVAEAGLE 224
Cdd:COG4913   235 DDLERAHEALEDAREQIEL-LEPIRELAE-----RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE 308
                          90
                  ....*....|....*...
gi 447201370  225 AQVSSAKAQLDQAQTTKD 242
Cdd:COG4913   309 AELERLEARLDALREELD 326
PRK09039 PRK09039
peptidoglycan -binding protein;
121-238 4.33e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.79  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 121 QAASGVEQAKNTLANQTQSIAQ----KQADIVAAQAKVEQVRAQYELSLAQLRRYQQLGNSGAASKSEQDKAAADAENNL 196
Cdd:PRK09039  46 REISGKDSALDRLNSQIAELADllslERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQEL 125
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 447201370 197 AALKQAEANVLvAKEALKTAQVAEagLEAQVSSAKAQLDQAQ 238
Cdd:PRK09039 126 DSEKQVSARAL-AQVELLNQQIAA--LRRQLAALEAALDASE 164
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
126-238 6.17e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 6.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 126 VEQAKNTLANQTQSIAQKQADIVAAQAKVEQVRAQYELSLAQLRRYQQLgnsgaASKSEQDKAAADAENNLAALKQAEAN 205
Cdd:COG4717   76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL-----LQLLPLYQELEALEAELAELPERLEE 150
                         90       100       110
                 ....*....|....*....|....*....|...
gi 447201370 206 VLVAKEALKTAQVAEAGLEAQVSSAKAQLDQAQ 238
Cdd:COG4717  151 LEERLEELRELEEELEELEAELAELQEELEELL 183
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
140-236 7.01e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 36.52  E-value: 7.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447201370 140 IAQKQADIVAAQAKVEQVRAQYELSLAQLRRyqqlgnsgaasKSEQDKAAADAE-NNLAALKQAEANvlvaKEALKTAQV 218
Cdd:PRK07353  41 IRTNRAEAKERLAEAEKLEAQYEQQLASARK-----------QAQAVIAEAEAEaDKLAAEALAEAQ----AEAQASKEK 105
                         90
                 ....*....|....*...
gi 447201370 219 AEAGLEAQVSSAKAQLDQ 236
Cdd:PRK07353 106 ARREIEQQKQAALAQLEQ 123
 
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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