|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
2-383 |
1.06e-91 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 281.60 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 2 SRRILPLFASLCMTAVLA--GCSDggessQTAGQGAARPPSpVSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIR 79
Cdd:PRK15030 4 NRGFTPLAVVLMLSGSLAltGCDD-----KQAQQGGQQMPA-VGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 80 DIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-ATQIEYENAKVTLLQAEADV 158
Cdd:PRK15030 78 KRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQyISKQEYDQALADAQQANAAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 159 AQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTTALTTLRRIDPIYIDLMESSINLLRLKKAISSGQLGG 238
Cdd:PRK15030 158 TAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 239 DTKETGIHLTLEDGTEYKHDGKIDMSDMAVSETTGTFSIRALFDNPDDLLLPGTYVRATLTIG-KETGFRIPQRAASRNA 317
Cdd:PRK15030 238 ENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGlNPNAILVPQQGVTRTP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489612414 318 NGELTAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVDGFQWIADGATVAPVEVTIDDR 383
Cdd:PRK15030 318 RGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNN 383
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
48-377 |
2.76e-83 |
|
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: 257.18 E-value: 2.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 48 KTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQAN 127
Cdd:COG0845 4 ERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 128 LARYERLVNSGA-TQIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQttALTT 206
Cdd:COG0845 84 LERYKALLKKGAvSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT--PLFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 207 LRRIDPIYIDLMESSINLLRLKKaissgqlgGDTketgIHLTLEDGTEYKHDGKIDMSDMAVSETTGTFSIRALFDNPDD 286
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARLKV--------GQP----VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 287 LLLPGTYVRATLTIGK-ETGFRIPQRAASRNANGeltaKFV---TAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVD 362
Cdd:COG0845 230 LLRPGMFVRVRIVLGErENALLVPASAVVRDGGG----AYVfvvDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVS 305
|
330
....*....|....*
gi 489612414 363 GFQWIADGATVAPVE 377
Cdd:COG0845 306 GLQRLRDGAKVRVVE 320
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
42-376 |
1.39e-66 |
|
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: 214.49 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 42 VSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASV 121
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 122 PSAQANLARYERLV-NSGATQIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQ 200
Cdd:TIGR01730 81 ELAQRSFERAERLVkRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 201 TtaLTTLRRIDPIYIDLMESSINLLRLKKaissgqlgGDTKEtgIHLTLEDGTEYKhdGKIDMSDMAVSETTGTFSIRAL 280
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQLRR--------GQTLT--VELDALPGEEFK--GKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 281 FDNPDDLLLPGTYVRATLTIG-KETGFRIPQRAASRNANGeltaKFVTA---ENKVETRTFPSSQQSGNAWLVTENVKDG 356
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKvRSSAIVVPTQAVIEDLNG----KYVYVvknDGKVSKRPVEVGLRNGGYVEIESGLKAG 302
|
330 340
....*....|....*....|
gi 489612414 357 DKLIVDGFQWIADGATVAPV 376
Cdd:TIGR01730 303 DQIVTAGVVKLRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
51-361 |
6.03e-51 |
|
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: 173.76 E-value: 6.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 51 EYPLTTVLPGRASAFQTAE-IRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLA 129
Cdd:pfam00529 3 PLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 130 RYERLVNSGAT-QIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTTALTTLR 208
Cdd:pfam00529 83 RLQALESELAIsRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 209 RIDPIYIDLMESSINLLRL-KKAISSGQLGGDTKETGIHLTLEDGTEYK----HDGKIDMSDMAVSETTGTFSIRALFDN 283
Cdd:pfam00529 163 QLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEirapVDGTVAFLSVTVDGGTVSAGLRLMFVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 284 PDD-LLLPGTYVRATL-TIGKETGFRIPQRAASRNANGELTAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIV 361
Cdd:pfam00529 243 PEDnLLVPGMFVETQLdQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
2-383 |
1.06e-91 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 281.60 E-value: 1.06e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 2 SRRILPLFASLCMTAVLA--GCSDggessQTAGQGAARPPSpVSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIR 79
Cdd:PRK15030 4 NRGFTPLAVVLMLSGSLAltGCDD-----KQAQQGGQQMPA-VGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 80 DIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-ATQIEYENAKVTLLQAEADV 158
Cdd:PRK15030 78 KRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQyISKQEYDQALADAQQANAAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 159 AQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTTALTTLRRIDPIYIDLMESSINLLRLKKAISSGQLGG 238
Cdd:PRK15030 158 TAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 239 DTKETGIHLTLEDGTEYKHDGKIDMSDMAVSETTGTFSIRALFDNPDDLLLPGTYVRATLTIG-KETGFRIPQRAASRNA 317
Cdd:PRK15030 238 ENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGlNPNAILVPQQGVTRTP 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489612414 318 NGELTAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVDGFQWIADGATVAPVEVTIDDR 383
Cdd:PRK15030 318 RGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEVTADNN 383
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
48-377 |
2.76e-83 |
|
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: 257.18 E-value: 2.76e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 48 KTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQAN 127
Cdd:COG0845 4 ERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 128 LARYERLVNSGA-TQIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQttALTT 206
Cdd:COG0845 84 LERYKALLKKGAvSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT--PLFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 207 LRRIDPIYIDLMESSINLLRLKKaissgqlgGDTketgIHLTLEDGTEYKHDGKIDMSDMAVSETTGTFSIRALFDNPDD 286
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARLKV--------GQP----VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 287 LLLPGTYVRATLTIGK-ETGFRIPQRAASRNANGeltaKFV---TAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVD 362
Cdd:COG0845 230 LLRPGMFVRVRIVLGErENALLVPASAVVRDGGG----AYVfvvDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVS 305
|
330
....*....|....*
gi 489612414 363 GFQWIADGATVAPVE 377
Cdd:COG0845 306 GLQRLRDGAKVRVVE 320
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-370 |
1.14e-82 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 258.11 E-value: 1.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 1 MSRRILPLFASLCMTAVLAGCSDggessQTAGQGAARPPSpVSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRD 80
Cdd:PRK09859 1 MNRRRKLLIPLLFCGAMLTACDD-----KSAENAAAMTPE-VGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 81 IPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-ATQIEYENAKVTLLQAEADVA 159
Cdd:PRK09859 75 RNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNyVSRQDYDTARTQLNEAEANVT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 160 QTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTTALTTLRRIDPIYIDLMESSINLLRLKKAISSGQLGGD 239
Cdd:PRK09859 155 VAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 240 TKETGIHLTLEDGTEYKHDGKIDMSDMAVSETTGTFSIRALFDNPDDLLLPGTYVRATLTIG-KETGFRIPQRAASRNAN 318
Cdd:PRK09859 235 QGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGsRQNVLLVPQEGVTHNAQ 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489612414 319 GELTAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVDGFQWIADG 370
Cdd:PRK09859 315 GKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
3-377 |
4.79e-71 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 227.75 E-value: 4.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 3 RRILPLFASLCMTAvLAGCSDGGEssqtaGQGAARPPSpVSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRDIP 82
Cdd:PRK09578 6 RRRLLLAALVALFV-LAGCGKGDS-----DAAAAAPRE-ATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTART 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 83 FKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSGA-TQIEYENAKVTLLQAEADVAQT 161
Cdd:PRK09578 79 YEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAvSERDYTEAVADERQAKAAVASA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 162 KAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTTALTTLRRIDPIYIDLMESSINLLRLKKAISSGQLGG-DT 240
Cdd:PRK09578 159 KAELARAQLQLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATGiAQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 241 KETGIHLTLEDGTEYKHDGKIDMSDMAVSETTGTFSIRALFDNPDDLLLPGTYVRATLTIG-KETGFRIPQRAASRNAnG 319
Cdd:PRK09578 239 QDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAvNPRAILVPRDALLRTA-D 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489612414 320 ELTAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVDGFQWIADGATVAPVE 377
Cdd:PRK09578 318 SASVKVVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVE 375
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
42-376 |
1.39e-66 |
|
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: 214.49 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 42 VSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASV 121
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 122 PSAQANLARYERLV-NSGATQIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQ 200
Cdd:TIGR01730 81 ELAQRSFERAERLVkRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 201 TtaLTTLRRIDPIYIDLMESSINLLRLKKaissgqlgGDTKEtgIHLTLEDGTEYKhdGKIDMSDMAVSETTGTFSIRAL 280
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQLRR--------GQTLT--VELDALPGEEFK--GKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 281 FDNPDDLLLPGTYVRATLTIG-KETGFRIPQRAASRNANGeltaKFVTA---ENKVETRTFPSSQQSGNAWLVTENVKDG 356
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKvRSSAIVVPTQAVIEDLNG----KYVYVvknDGKVSKRPVEVGLRNGGYVEIESGLKAG 302
|
330 340
....*....|....*....|
gi 489612414 357 DKLIVDGFQWIADGATVAPV 376
Cdd:TIGR01730 303 DQIVTAGVVKLRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
51-361 |
6.03e-51 |
|
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: 173.76 E-value: 6.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 51 EYPLTTVLPGRASAFQTAE-IRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLA 129
Cdd:pfam00529 3 PLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 130 RYERLVNSGAT-QIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTTALTTLR 208
Cdd:pfam00529 83 RLQALESELAIsRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 209 RIDPIYIDLMESSINLLRL-KKAISSGQLGGDTKETGIHLTLEDGTEYK----HDGKIDMSDMAVSETTGTFSIRALFDN 283
Cdd:pfam00529 163 QLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEAELKLAKLDLERTEirapVDGTVAFLSVTVDGGTVSAGLRLMFVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 284 PDD-LLLPGTYVRATL-TIGKETGFRIPQRAASRNANGELTAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIV 361
Cdd:pfam00529 243 PEDnLLVPGMFVETQLdQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
22-377 |
1.58e-37 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 140.31 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 22 SDGGESSQTAGQGAAR------PPSPVSIIVMKTSEYPLTTVLPGRASAFQTAEIRPRVTGIIRDIPFKEGSEVKQGDIL 95
Cdd:PRK11556 36 APGAAKQAQQSPAGGRrgmrsgPLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 96 YQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-ATQIEYENAKVTLLQAEADVAQTKAALETAEINLDL 174
Cdd:PRK11556 116 AEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNlVSRQELDAQQALVSETEGTIKADEASVASAQLQLDY 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 175 TKVRAPFDGITSATAFSIGNVVTANQTTALTTLRRIDPIYI--DLMESSINllRLKKAISSGQ-LGGDTKETGIHLTLED 251
Cdd:PRK11556 196 SRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLvfTLPESDIA--TVVQAQKAGKpLVVEAWDRTNSKKLSE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 252 GTEYKHDGKIDmsdmavsETTGTFSIRALFDNPDDLLLPGTYVRATLTIGKETGFRIPQRAASRNANgelTAKFV---TA 328
Cdd:PRK11556 274 GTLLSLDNQID-------ATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGN---EGHFVwvlND 343
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 489612414 329 ENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVDGFQWIADGATVAPVE 377
Cdd:PRK11556 344 ENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVE 392
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
42-301 |
6.29e-27 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 109.37 E-value: 6.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 42 VSIIVMKTSEYPLTTVLPGRASAfQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASV 121
Cdd:COG1566 21 LALWAAGRNGPDEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 122 PS---------------------------AQANLARYERLVNSGA-TQIEYENAKVTLLQA------------------- 154
Cdd:COG1566 100 ARleaelgaeaeiaaaeaqlaaaqaqldlAQRELERYQALYKKGAvSQQELDEARAALDAAqaqleaaqaqlaqaqaglr 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 155 --------EADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQTtaLTTLRRIDPIYIDLM--ESSINL 224
Cdd:COG1566 180 eeeelaaaQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYvpETDLGR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 225 LRLkkaissGQlggdtkETGIHLTLEDGTEYKhdGKID----------MSDMAVSETTGTFSIRALFDNPDDLLL-PGTY 293
Cdd:COG1566 258 VKP------GQ------PVEVRVDAYPDRVFE--GKVTsispgagftsPPKNATGNVVQRYPVRIRLDNPDPEPLrPGMS 323
|
....*...
gi 489612414 294 VRATLTIG 301
Cdd:COG1566 324 ATVEIDTE 331
|
|
| 8a0102 |
TIGR00999 |
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ... |
86-363 |
2.01e-16 |
|
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]
Pssm-ID: 273386 [Multi-domain] Cd Length: 265 Bit Score: 78.64 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 86 GSEVKQGDILYQIedntYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSGAT-QIEYENAKVTLLQAEADVAQTKAA 164
Cdd:TIGR00999 1 GDPVKKGQVLAVV----DSPELAKMAAELKVAQKRVELARKTYEREKKLFEQGVIpRQEFESAEYALEEAQAEVQAAKSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 165 LETAEINLD--LTKVRAPFDGITSATAFSIGNVVTANQTtaLTTLRRIDPIYIDLMESSINLLRLKKaissgqlgGDTKE 242
Cdd:TIGR00999 77 LRSAREAKDgsYVEVRSPFDGYITQKSVTLGDYVAPQAE--LFRVADLGAVWVEAEVPAKDVSRIRK--------GSKAT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 243 tgihLTLEDGTEYkhDGKIDMSDMAVSETTGTFSIRALFDNPDDLLLPGTYVRATL-TIGKETGFRIPQRAAsRNANGEl 321
Cdd:TIGR00999 147 ----VLLENGRPL--PARVDYVGPEVDGSSRTAKVRVLIKNENLTLKPGLFVQVRVeTKIGEPAIAVPEDAV-QDLGGR- 218
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489612414 322 TAKFVTAENKVETRTFPSSQQSGNAWLVTENVKDGDKLIVDG 363
Cdd:TIGR00999 219 KVVFVRTQEGFRPRPVKVGRRLGGYYEVLEGLKPGERVAVEN 260
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
48-201 |
5.69e-16 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 78.53 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 48 KTSEYPLTTvlPGRASAfQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEAS------- 120
Cdd:PRK10476 32 RTDSAPSTD--DAYIDA-DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQimttqrs 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 121 --------------VPSAQANLA-------RYERLVNSG-ATQIEYENAKV-----------TLLQ-------------A 154
Cdd:PRK10476 109 vdaersnaasaneqVERARANAKlatrtleRLEPLLAKGyVSAQQVDQARTaqrdaevslnqALLQaqaaaaavggvdaL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489612414 155 EADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVTANQT 201
Cdd:PRK10476 189 VAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQP 235
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
70-183 |
5.32e-12 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 66.30 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 70 IRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSGATQIEYENAKV 149
Cdd:PRK10559 50 IAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANN 129
|
90 100 110
....*....|....*....|....*....|....
gi 489612414 150 TLLQAEADVAQTKAALETAEINLDLTKVRAPFDG 183
Cdd:PRK10559 130 VLQTVLHQLAKAQATRDLAKLDLERTVIRAPADG 163
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
73-215 |
2.75e-09 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 58.05 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 73 RVTGIIRDIPFKEGSEVKQGDILYQIEDNTYL--------------------------AEVAQAKASVAKAEASVPSAQA 126
Cdd:PRK03598 49 RVGGRLASLAVDEGDAVKAGQVLGELDAAPYEnalmqakanvsvaqaqldlmlagyrdEEIAQARAAVKQAQAAYDYAQN 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 127 NLARYERLVNSGAT-QIEYENAKVT--------------------------LLQAEADVAQTKAALETAEINLDLTKVRA 179
Cdd:PRK03598 129 FYNRQQGLWKSRTIsANDLENARSSrdqaqatlksaqdklsqyregnrpqdIAQAKASLAQAQAALAQAELNLQDTELIA 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 489612414 180 PFDGITSATAFSIGNVVTAnQTTALtTLRRIDPIYI 215
Cdd:PRK03598 209 PSDGTILTRAVEPGTMLNA-GSTVF-TLSLTRPVWV 242
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
60-228 |
4.05e-09 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 57.86 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 60 GRASAFQTAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASV-------AKAEASVPSAQANLARYE 132
Cdd:PRK11578 54 GKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLmelraqrQQAEAELKLARVTLSRQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 133 RL----------VNSGATQIEYENAKVTLLQAEadVAQTKAALETAEINLDLTKVRAPFDG-ITSATAFSIGNVVTANQT 201
Cdd:PRK11578 134 RLaktqavsqqdLDTAATELAVKQAQIGTIDAQ--IKRNQASLDTAKTNLDYTRIVAPMAGeVTQITTLQGQTVIAAQQA 211
|
170 180
....*....|....*....|....*..
gi 489612414 202 TALTTLRRIDPIYIDLMESSINLLRLK 228
Cdd:PRK11578 212 PNILTLADMSTMLVKAQVSEADVIHLK 238
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
67-115 |
2.32e-08 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 49.75 E-value: 2.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 489612414 67 TAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVA 115
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
80-178 |
9.97e-06 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 47.34 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 80 DIPFKEGSEVKQGDILYQIEDNTY-------LAEVAQAKASVAKAEASVPSAQANLARYERLVNsgATQIEYENAKVT-- 150
Cdd:COG1538 44 DLGGKRRARIEAAKAQAEAAEADLraarldlAAEVAQAYFDLLAAQEQLALAEENLALAEELLE--LARARYEAGLASrl 121
|
90 100
....*....|....*....|....*....
gi 489612414 151 -LLQAEADVAQTKAALETAEINLDLTKVR 178
Cdd:COG1538 122 dVLQAEAQLAQARAQLAQAEAQLAQARNA 150
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
93-172 |
5.75e-05 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 44.64 E-value: 5.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 93 DILYQIEDNtyLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-ATQIEYENAKVTLLQAEADVAQTKAALETAEIN 171
Cdd:COG1538 280 QALQEVEDA--LAALRAAREQLEALEEALEAAEEALELARARYRAGlASLLDVLDAQRELLQAQLNLIQARYDYLLALVQ 357
|
.
gi 489612414 172 L 172
Cdd:COG1538 358 L 358
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
97-172 |
5.78e-05 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 43.66 E-value: 5.78e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489612414 97 QIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-ATQIEYENAKVTLLQAEADVAQTKAALETAEINL 172
Cdd:pfam02321 100 RLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGlISLLDVLQAEVELLEARLELLNAEADLELALAQL 176
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
104-201 |
8.41e-05 |
|
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: 44.62 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 104 LAEVAQAKASVAKAEASVPSAQANLARYERLVnSGATQIEYENAKVTLLQAEADVAQTKAALETAEINLDLTKVRAPFDG 183
Cdd:TIGR01843 202 ERERAEAQGELGRLEAELEVLKRQIDELQLER-QQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDG 280
|
90
....*....|....*....
gi 489612414 184 -ITSATAFSIGNVVTANQT 201
Cdd:TIGR01843 281 tVQSLKVHTVGGVVQPGET 299
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
69-188 |
1.38e-04 |
|
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: 43.84 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 69 EIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDntylaevAQAKASVAKAEASVPSAQANLARYERLVNSgATQIEYENAK 148
Cdd:TIGR01843 45 VVQHLEGGIVREILVREGDRVKAGQVLVELDA-------TDVEADAAELESQVLRLEAEVARLRAEADS-QAAIEFPDDL 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489612414 149 VT---------LLQAEADVAQTKAAL--ETAEINLDLTKVRAPFDGITSAT 188
Cdd:TIGR01843 117 LSaedpavpelIKGQQSLFESRKSTLraQLELILAQIKQLEAELAGLQAQL 167
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
83-178 |
7.73e-04 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 40.20 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 83 FKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSG-----ATQIEYENAKVT---LLQA 154
Cdd:pfam02321 72 GKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAeealeLAEARYEAGLISlldVLQA 151
|
90 100
....*....|....*....|....
gi 489612414 155 EADVAQTKAALETAEINLDLTKVR 178
Cdd:pfam02321 152 EVELLEARLELLNAEADLELALAQ 175
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
176-291 |
1.08e-03 |
|
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: 38.11 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 176 KVRAPFDGITSATAFSIGNVVTANQTtaLTTLRRIDPIYIDLmessinllrlkkAISSGQLGGDTKETGIHLTLEDGTEY 255
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDP--LATIVPPDRLLVEA------------FVPAADLGSLKKGQKVTLKLDPGSDY 66
|
90 100 110
....*....|....*....|....*....|....*...
gi 489612414 256 KHDGKIDMSDMAVSETTGTFSIRALFDNP--DDLLLPG 291
Cdd:pfam13437 67 TLEGKVVRISPTVDPDTGVIPVRVSIENPktPIPLLPG 104
|
|
| aceF |
PRK11854 |
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated |
51-197 |
1.09e-03 |
|
pyruvate dehydrogenase dihydrolipoyltransacetylase; Validated
Pssm-ID: 236999 [Multi-domain] Cd Length: 633 Bit Score: 41.14 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 51 EYPLTTVLPGRASAfqtaEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLAR 130
Cdd:PRK11854 31 EQSLITVEGDKASM----EVPSPQAGVVKEIKVKVGDKVETGALIMIFESADGAADAAPAQAEEKKEAAPAAAPAAAAAK 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489612414 131 YERLVNSGATQIEyenakVT-LLQAEADVAQTKAALETAEINLDLTKVRAPFDGITSATAFSIGNVVT 197
Cdd:PRK11854 107 DVHVPDIGSDEVE-----VTeILVKVGDTVEAEQSLITVEGDKASMEVPAPFAGTVKEIKVNVGDKVS 169
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
67-129 |
3.34e-03 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 39.42 E-value: 3.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489612414 67 TAEIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLA 129
Cdd:PRK11855 161 TMEIPSPVAGVVKEIKVKVGDKVSVGSLLVVIEVAAAAPAAAAAPAAAAPAAAAAAAPAPAPA 223
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
101-179 |
3.90e-03 |
|
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: 38.94 E-value: 3.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489612414 101 NTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNSGAtQIEYENAKVTLLQAEADVAQTKAALetAEINLDLTKVRA 179
Cdd:TIGR04320 278 NTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTA-QNNLATAQAALANAEARLAKAKEAL--ANLNADLAKKQA 353
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
69-147 |
8.32e-03 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 38.18 E-value: 8.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489612414 69 EIRPRVTGIIRDIPFKEGSEVKQGDILYQIEDNTYLAEVAQAKASVAKAEASVPSAQANLARYERLVNS--GATQIEYEN 146
Cdd:TIGR01347 45 EVPSPADGVLQEILFKEGDTVESGQVLAILEEGNDATAAPPAKSGEEKEETPAASAAAAPTAAANRPSLspAARRLAKEH 124
|
.
gi 489612414 147 A 147
Cdd:TIGR01347 125 G 125
|
|
| |
