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Conserved domains on  [gi|1915222241|dbj|BBV80902|]
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macrolide transporter subunit MacA [Enterobacter kobei]

Protein Classification

macrolide transporter subunit MacA( domain architecture ID 11485414)

macrolide transporter subunit MacA stimulates the ATPase activity of MacB by promoting the closed ATP-bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 1-370 0e+00

macrolide transporter subunit MacA; Provisional


:

Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 641.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   1 MNLKGKRRTLFLLLAVVILVGGFWLWQVLNAPVPQYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIG 80
Cdd:PRK11578    1 MKKRKKVKKRYLIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  81 DKVKKGQLLGVIDPEQAENQIREVEATLMELRAQRAQAQAERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQAQI 160
Cdd:PRK11578   81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 161 GTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
Cdd:PRK11578  161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 241 QNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGESAGD 320
Cdd:PRK11578  241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGD 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1915222241 321 NRYKVKVLRNGETRDREVVIGARNDTDVVVVKGLEEGEEVVVSESLPGAA 370
Cdd:PRK11578  321 NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKPGAA 370
 
Name Accession Description Interval E-value
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 1-370 0e+00

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 641.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   1 MNLKGKRRTLFLLLAVVILVGGFWLWQVLNAPVPQYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIG 80
Cdd:PRK11578    1 MKKRKKVKKRYLIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  81 DKVKKGQLLGVIDPEQAENQIREVEATLMELRAQRAQAQAERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQAQI 160
Cdd:PRK11578   81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 161 GTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
Cdd:PRK11578  161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 241 QNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGESAGD 320
Cdd:PRK11578  241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGD 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1915222241 321 NRYKVKVLRNGETRDREVVIGARNDTDVVVVKGLEEGEEVVVSESLPGAA 370
Cdd:PRK11578  321 NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKPGAA 370
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 41-354 3.89e-73

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: 230.22  E-value: 3.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  41 VRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPeqaenqiREVEATLMELRAQRAQAQA 120
Cdd:COG0845     3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDP-------PDLQAALAQAQAQLAAAQA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 121 ERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQaqigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTL 200
Cdd:COG0845    76 QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQ-------AALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 201 QGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAifYYARFE 280
Cdd:COG0845   149 PGQLVSAGTP---LFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRT--VRVRAE 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915222241 281 VPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGESAGDNRykVKVLRNGET-RDREVVIGARNDTDVVVVKGL 354
Cdd:COG0845   224 LPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAY--VFVVDADGKvERRPVTLGRRDGDQVEVLSGL 296
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 38-354 2.05e-49

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: 168.65  E-value: 2.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  38 TLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPeqaenqiREVEATLMELRAQRAQ 117
Cdd:TIGR01730   3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDD-------DDYQLALQAALAQLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 118 AQAERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQaqigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQI 197
Cdd:TIGR01730  76 AEAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQ-------ADLEAAKASLASAQLNLRYTEIRAPFDGTIGRR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 198 TTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYA 277
Cdd:TIGR01730 149 LVEVGAYVTAGQ---TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRA 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915222241 278 RFevPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGEsaGDNRYKVKVLRN-GETRDREVVIGARNDTDVVVVKGL 354
Cdd:TIGR01730 226 TF--PNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIE--DLNGKYVYVVKNdGKVSKRPVEVGLRNGGYVEIESGL 299
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 43-235 8.29e-19

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: 85.94  E-value: 8.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  43 PGELQQNVLATGKLDALRKVD-VGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAENQIREVEATLMELRAQRAQAQAE 121
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 122 RNlaqvtltRQQALAKTQAISKQDLDTATTELavKQAQigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQ 201
Cdd:pfam00529  81 LD-------RLQALESELAISRQDYDGATAQL--RAAQ-----AAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTA 146

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1915222241 202 GQTVIAAQQAPNIlTLADMSTMLVKAQVSEADVI 235
Cdd:pfam00529 147 GALVAQAQANLLA-TVAQLDQIYVQITQSAAENQ 179
 
Name Accession Description Interval E-value
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 1-370 0e+00

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 641.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   1 MNLKGKRRTLFLLLAVVILVGGFWLWQVLNAPVPQYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIG 80
Cdd:PRK11578    1 MKKRKKVKKRYLIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  81 DKVKKGQLLGVIDPEQAENQIREVEATLMELRAQRAQAQAERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQAQI 160
Cdd:PRK11578   81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 161 GTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
Cdd:PRK11578  161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 241 QNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGESAGD 320
Cdd:PRK11578  241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGD 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1915222241 321 NRYKVKVLRNGETRDREVVIGARNDTDVVVVKGLEEGEEVVVSESLPGAA 370
Cdd:PRK11578  321 NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKPGAA 370
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 41-354 3.89e-73

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: 230.22  E-value: 3.89e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  41 VRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPeqaenqiREVEATLMELRAQRAQAQA 120
Cdd:COG0845     3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDP-------PDLQAALAQAQAQLAAAQA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 121 ERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQaqigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTL 200
Cdd:COG0845    76 QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQ-------AALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 201 QGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAifYYARFE 280
Cdd:COG0845   149 PGQLVSAGTP---LFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRT--VRVRAE 223

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915222241 281 VPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGESAGDNRykVKVLRNGET-RDREVVIGARNDTDVVVVKGL 354
Cdd:COG0845   224 LPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAY--VFVVDADGKvERRPVTLGRRDGDQVEVLSGL 296
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 38-354 2.05e-49

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: 168.65  E-value: 2.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  38 TLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPeqaenqiREVEATLMELRAQRAQ 117
Cdd:TIGR01730   3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDD-------DDYQLALQAALAQLAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 118 AQAERNLAQVTLTRQQALAKTQAISKQDLDTATTELAVKQaqigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQI 197
Cdd:TIGR01730  76 AEAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQ-------ADLEAAKASLASAQLNLRYTEIRAPFDGTIGRR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 198 TTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIFYYA 277
Cdd:TIGR01730 149 LVEVGAYVTAGQ---TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRA 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915222241 278 RFevPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGEsaGDNRYKVKVLRN-GETRDREVVIGARNDTDVVVVKGL 354
Cdd:TIGR01730 226 TF--PNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIE--DLNGKYVYVVKNdGKVSKRPVEVGLRNGGYVEIESGL 299
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
1-300 4.83e-49

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 167.92  E-value: 4.83e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   1 MNLKGKRRTLFLLLAVVILVGGFWLWQVLNAPVPqyrtlivrpgelqqnVLATGKLDAlRKVDVGAQVSGQLKTLSVEIG 80
Cdd:COG1566     1 MKALKKRRLLALVLLLLALGLALWAAGRNGPDEP---------------VTADGRVEA-RVVTVAAKVSGRVTEVLVKEG 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  81 DKVKKGQLLGVIDPEQAENQIREVEATL--------------------MELRAQRAQAQAERNLAQVTLTRQQALAKTQA 140
Cdd:COG1566    65 DRVKKGQVLARLDPTDLQAALAQAEAQLaaaeaqlarleaelgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 141 ISKQDLDTATTELAVKQAQ--------------------IGTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTL 200
Cdd:COG1566   145 VSQQELDEARAALDAAQAQleaaqaqlaqaqaglreeeeLAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVE 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 201 QGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPEKV--------NDA 272
Cdd:COG1566   225 PGEVVSAGQP---LLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTsppknatgNVV 301

                         330       340
                  ....*....|....*....|....*....
gi 1915222241 273 IFYYARFEVPNPQGV-LRLDMTAQVHIQL 300
Cdd:COG1566   302 QRYPVRIRLDNPDPEpLRPGMSATVEIDT 330
PRK10476 PRK10476
multidrug transporter subunit MdtN;
6-262 6.67e-23

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 98.18  E-value: 6.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   6 KRRTLFLLLAVVILVGGFWLWQVLNAPVPQyrtlivrpgelqqnvlaTGKLDAlRKVDVGAQVSGQLKTLSVEIGDKVKK 85
Cdd:PRK10476   11 KKLPALAIVALAIVALVFVIWRTDSAPSTD-----------------DAYIDA-DVVHVASEVGGRIVELAVTENQAVKK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  86 GQLLGVIDP-------EQAENQIREVEATLMELR--------------AQRAQAQAERNLAQVTLTRQQALAKTQAISKQ 144
Cdd:PRK10476   73 GDLLFRIDPrpyeltvAQAQADLALADAQIMTTQrsvdaersnaasanEQVERARANAKLATRTLERLEPLLAKGYVSAQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 145 DLDTATT-----ELAVKQAQ---------IGTID---AQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIA 207
Cdd:PRK10476  153 QVDQARTaqrdaEVSLNQALlqaqaaaaaVGGVDalvAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAP 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1915222241 208 AQqapNILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDI 262
Cdd:PRK10476  233 MQ---PIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSI 284
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 7-267 1.43e-21

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 93.87  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   7 RRTLFLLLAVVILV----GGFWLWQvlnapvPQYRTLIVrpgeLQQNVlatgkldALRKVDVGAQVSGQLKTLSVEIGDK 82
Cdd:PRK03598    2 KKKVVIGLAVVVLAaavaGGWWWYQ------SRQDNGLT----LYGNV-------DIRTVNLGFRVGGRLASLAVDEGDA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  83 VKKGQLLGVIDPEQAENQIREVEATLMELRAQRA-------------------QAQAERNLAQVTLTRQQALAKTQAISK 143
Cdd:PRK03598   65 VKAGQVLGELDAAPYENALMQAKANVSVAQAQLDlmlagyrdeeiaqaraavkQAQAAYDYAQNFYNRQQGLWKSRTISA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 144 QDLDTATTELAVKQAQ-------------------IGTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGqT 204
Cdd:PRK03598  145 NDLENARSSRDQAQATlksaqdklsqyregnrpqdIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPG-T 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915222241 205 VIAAQQApnILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPE 267
Cdd:PRK03598  224 MLNAGST--VFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAE 284
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
1-194 5.25e-20

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 90.62  E-value: 5.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   1 MNLKGKRRTLFLLLAVVILVGGFWLWQVLNAPVPQY-------------RTLIVRPGEL---------QQNV----LATG 54
Cdd:PRK11556    1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAApgaakqaqqspagGRRGMRSGPLapvqaatatEQAVprylTGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  55 KLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPeqaenqiREVEATLMELRAQRAQAQAERNLAQVTLTRQQA 134
Cdd:PRK11556   81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDP-------RPFKVALAQAQGQLAKDQATLANARRDLARYQQ 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 135 LAKTQAISKQDLDTattelavKQAQIGTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEV 194
Cdd:PRK11556  154 LAKTNLVSRQELDA-------QQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRV 206
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 43-235 8.29e-19

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: 85.94  E-value: 8.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  43 PGELQQNVLATGKLDALRKVD-VGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAENQIREVEATLMELRAQRAQAQAE 121
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 122 RNlaqvtltRQQALAKTQAISKQDLDTATTELavKQAQigtidAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQ 201
Cdd:pfam00529  81 LD-------RLQALESELAISRQDYDGATAQL--RAAQ-----AAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTA 146

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1915222241 202 GQTVIAAQQAPNIlTLADMSTMLVKAQVSEADVI 235
Cdd:pfam00529 147 GALVAQAQANLLA-TVAQLDQIYVQITQSAAENQ 179
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 45-294 5.21e-16

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: 76.01  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  45 ELQQNVLATGKL--DALRKVDVGAQVSGQLKTLSV-EIGDKVKKGQLLGVID-PEQAENQirevEATLMELRAQRAQAQA 120
Cdd:pfam16576   1 PLSRTIRAVGRVayDERRLAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYsPELVAAQ----QEYLLALRSGDALSKS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 121 ERnlaqvtltRQQALAKTQAiskqdldtatteLAVKQAQIgtidAQIKRNQasldTAKTNLDytqIVAPMAGEVTQITTL 200
Cdd:pfam16576  77 EL--------LRAARQRLRL------------LGMPEAQI----AELERTG----KVQPTVT---VYAPISGVVTELNVR 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 201 QGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPTPEKVNDAIfyYARFE 280
Cdd:pfam16576 126 EGMYVQPGD---TLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTV--RVRIE 200

                         250
                  ....*....|....
gi 1915222241 281 VPNPQGVLRLDMTA 294
Cdd:pfam16576 201 LPNPDGRLKPGMFA 214
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
33-238 1.07e-15

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 77.83  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  33 VPQYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQaenqireVEATLMELR 112
Cdd:PRK15030   37 MPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPAT-------YQATYDSAK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 113 AQRAQAQAERNLAQVTLTRQQALAKTQAISKQDLDTATTElaVKQAqigtiDAQIKRNQASLDTAKTNLDYTQIVAPMAG 192
Cdd:PRK15030  110 GDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALAD--AQQA-----NAAVTAAKAAVETARINLAYTKVTSPISG 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1915222241 193 EVTQITTLQGqTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLK 238
Cdd:PRK15030  183 RIGKSNVTEG-ALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLK 227
PRK09859 PRK09859
multidrug transporter subunit MdtE;
31-318 5.48e-15

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 75.52  E-value: 5.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  31 APVPQYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEqaenqirEVEATLME 110
Cdd:PRK09859   31 AMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPA-------PLQAELNS 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 111 LRAQRAQAQAERNLAQVTLTRQQALAKTQAISKQDLDTATTelavkqaQIGTIDAQIKRNQASLDTAKTNLDYTQIVAPM 190
Cdd:PRK09859  104 AKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTART-------QLNEAEANVTVAKAAVEQATINLQYANVTSPI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 191 AGeVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKP-----------GQNAWFTVLGDPQtRYE--G 257
Cdd:PRK09859  177 TG-VSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEevasgqikqvqGSTPVQLNLENGK-RYSqtG 254

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915222241 258 VLKDILPTPEKVNDAIFYYARFevPNPQGVLRLDMTAQVHIQLTGVKNVLTIPLSALGESA 318
Cdd:PRK09859  255 TLKFSDPTVDETTGSVTLRAIF--PNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNA 313
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
5-354 6.41e-14

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 72.13  E-value: 6.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   5 GKRRTLFLLLAVVILVGGFWLWQVLNAP--VPQYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDK 82
Cdd:PRK09578    5 RRRRLLLAALVALFVLAGCGKGDSDAAAaaPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  83 VKKGQLLGVIDPEQaenqireVEATLMELRAQRAQAQAERNLAQVTLTRQQALAKTQAISKQDLDTATTElaVKQAQigt 162
Cdd:PRK09578   85 VKQGAVLFRIDPAP-------LKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVAD--ERQAK--- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 163 idAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTViaAQQAPNILTLAD-MSTMLVKAQVSEADVIHLKPG- 240
Cdd:PRK09578  153 --AAVASAKAELARAQLQLDYATVTAPIDGRARRALVTEGALV--GQDQATPLTTVEqLDPIYVNFSQPAADVEALRRAv 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 241 QNAWFTVLGDPQTRYEGVLKDILPTPEK------------VNDAIFYYARFevPNPQGVLRLDMTAQVHIQLTGVKNVLT 308
Cdd:PRK09578  229 KSGRATGIAQQDVAVTLVRADGSEYPLKgkllfsdlavdpTTDTVAMRALF--PNPERELLPGAYVRIALDRAVNPRAIL 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1915222241 309 IPLSALGESAGdnRYKVKVL-RNGETRDREVVIGARNDTDVVVVKGL 354
Cdd:PRK09578  307 VPRDALLRTAD--SASVKVVgQNGKVRDVEVEADQMSGRDWIVTRGL 351
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
 72-249 1.30e-12

ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.


Pssm-ID: 213754 [Multi-domain]  Cd Length: 327  Bit Score: 67.93  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  72 LKTLSVEIGDKVKKGQLLGVIDP--------EQAENQIREVEATLMELRAQRAQAQ------------------------ 119
Cdd:TIGR02971  27 IKKLLVAEGDRVQAGQVLAELDSrpertaelDVARTQLDEAKARLAQVRAGAKKGEiaaqraaraaaklfkdvaaqqatl 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 120 ----AERNLAQVTLTRQQALAKTQAISKQDLD------------------------------TATTELAVKQAQIGTIDA 165
Cdd:TIGR02971 107 nrleAELETAQREVDRYRSLFRDGAVSASDLDskalklrtaeeeleealasrseqidgaraaLASLAEEVRETDVDLAQA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 166 QIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTViaaqQAPNILTLADMSTMLVKAQVSEADVIHLKPGQNAWF 245
Cdd:TIGR02971 187 EVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGEVI----GSEGILEMGDTSQMYAVAEVYETDINRVRVGQRATI 262


                  ....
gi 1915222241 246 TVLG 249
Cdd:TIGR02971 263 TSTA 266
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 186-289 2.81e-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: 59.68  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 186 IVAPMAGEVTQITTLQGQtVIAAQQapNILTLADMSTMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGVLKDILPT 265
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQ-VVQAGD--PLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPT 78

                          90       100
                  ....*....|....*....|....
gi 1915222241 266 PEKVNDAIFYYARFEVPNPQGVLR 289
Cdd:pfam13437  79 VDPDTGVIPVRVSIENPKTPIPLL 102
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
2-250 9.52e-11

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 62.79  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   2 NLKGKRRTLFLLLAVV-ILVGGFWLwqvlnapvpQYRTLIVRPGELQQNVLATGKldalrKVDVGAQVSGQLKTLSVEIG 80
Cdd:PRK15136   15 KKKGKRKRALLLLTLLfIIIGVAYG---------IYWFLVLRHHQETDDAYVAGN-----QVQIMSQVSGSVTKVWADNT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  81 DKVKKGQLLGVIDPEQAE-----------NQIREVEATLM---ELRAQRAQAQAERNLAQVTLTRQQALAKTQAISKQDL 146
Cdd:PRK15136   81 DFVKEGDVLVTLDPTDAEqafekaktalaNSVRQTHQLMInskQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREEL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 147 DTATTELAVKQAQIGTIDAQIKRNQAS-LDT-----------------AKTNLDYTQIVAPMAGEVTQITTLQGqtviaA 208
Cdd:PRK15136  161 QHARDAVASAQAQLDVAIQQYNANQAMiLNTpledqpavqqaatevrnAWLALQRTKIVSPMTGYVSRRSVQVG-----A 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1915222241 209 QQAPN--ILTLADMSTMLVKAQVSEADVIHLKPGQNAwfTVLGD 250
Cdd:PRK15136  236 QISPTtpLMAVVPATNLWVDANFKETQLANMRIGQPA--TITSD 277
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
62-258 1.01e-08

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 55.90  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  62 VDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAENQIREVEAtlmELRAQRAQAQAERNLAQvtltRQQALAkTQAI 141
Cdd:PRK10559   48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEA---DVAYYQVLAQEKRREAG----RRNRLG-VQAM 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241 142 SKQDLDTATTELAvkqaqigTIDAQIKRNQASLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAAQQApniLTLADMS 221
Cdd:PRK10559  120 SREEIDQANNVLQ-------TVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA---VALVKQN 189

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1915222241 222 TMLVKAQVSEADVIHLKPGQNAWFTVLGDPQTRYEGV 258
Cdd:PRK10559  190 SFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTV 226
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
60-108 1.18e-05

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 42.04  E-value: 1.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1915222241  60 RKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAENQIREVEATL 108
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQL 49
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
90-188 7.84e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.99  E-value: 7.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  90 GVIDPE-QAENQIreveATLMELRAQRAQAQAERNLAQVTLTRQQAlaktqaiskqdldtattELAVKQAQIGTIDAQIK 168
Cdd:COG3524   208 GILDPEaTAEALL----QLIATLEGQLAELEAELAALRSYLSPNSP-----------------QVRQLRRRIAALEKQIA 266

                          90       100
                  ....*....|....*....|
gi 1915222241 169 RNQASLDTAKTNLDYTQIVA 188
Cdd:COG3524   267 AERARLTGASGGDSLASLLA 286
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
95-208 8.85e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 8.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  95 EQAENQIREVEATLMELRAQRAQAQAErnlaqvtltRQQALAKTQAISKQDLDTATTELAVKQAQIGTIDAQIKRNQASL 174
Cdd:COG4717   152 EERLEELRELEEELEELEAELAELQEE---------LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL 222

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1915222241 175 DTAKTNLDYTQIVAPMAGEVTQITTLQGQTVIAA 208
Cdd:COG4717   223 EELEEELEQLENELEAAALEERLKEARLLLLIAA 256
PRK12999 PRK12999
pyruvate carboxylase; Reviewed
 35-92 1.04e-03

pyruvate carboxylase; Reviewed


Pssm-ID: 237263 [Multi-domain]  Cd Length: 1146  Bit Score: 41.28  E-value: 1.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1915222241   35 QYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVI 92
Cdd:PRK12999  1050 QPREVQVRDRSVKSTVAAREKADPGNPGHVGAPMPGSVVTVLVKEGDEVKAGDPLAVI 1107
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
93-182 1.21e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 39.81  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  93 DPE-QAENQIREVEATLMELRAQRAQAQAERNLAQVTLTRQQALAKT------QAISKQDLDTATTELAVKQ---AQIGT 162
Cdd:COG1842    23 DPEkMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKweekarLALEKGREDLAREALERKAeleAQAEA 102

                          90       100
                  ....*....|....*....|
gi 1915222241 163 IDAQIKRNQASLDTAKTNLD 182
Cdd:COG1842   103 LEAQLAQLEEQVEKLKEALR 122
PRK11855 PRK11855
dihydrolipoamide acetyltransferase; Reviewed
 62-205 2.09e-03

dihydrolipoamide acetyltransferase; Reviewed


Pssm-ID: 237000 [Multi-domain]  Cd Length: 547  Bit Score: 40.19  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  62 VDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDPEQAENQIREVEAtlmelraqrAQAQAERNLAQVTLTRQQALAKTQAI 141
Cdd:PRK11855   45 MEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAAAAAAAPAA---------AAAPAAAAAAAPAPAAAAPAAAAAAA 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915222241 142 SKQDLDtattelaVKQAQIGTIDA------------QIKRNQaSLDTAKTNLDYTQIVAPMAGEVTQITTLQGQTV 205
Cdd:PRK11855  116 GGGVVE-------VKVPDIGEITEveviewlvkvgdTVEEDQ-SLITVETDKATMEIPSPVAGVVKEIKVKVGDKV 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 98-186 2.13e-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: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  98 ENQIREVEATLMELRAQRAQAQAERNLAQVTLTRQqalaktqaisKQDLDTATTELAVKQAQIGTIDAQIKRNQASLDTA 177
Cdd:COG1579    16 DSELDRLEHRLKELPAELAELEDELAALEARLEAA----------KTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV 85


                  ....*....
gi 1915222241 178 KTNLDYTQI 186
Cdd:COG1579    86 RNNKEYEAL 94
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 57-175 2.34e-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: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  57 DALRKVDVGAQVSGQLKTLSV-----EIGDKVKKGQLLGVIDPEQAEnQIREVEATLMELRAQRAQAQAERNLAQVTLTR 131
Cdd:COG4942   104 EELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELAALRAELEAERAELEALLAE 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1915222241 132 QQALAKTQAISKQDLDTATTELAVKQAQIGTIDAQIKRNQASLD 175
Cdd:COG4942   183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-182 2.60e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  95 EQAENQIREVEATLMELRAQRAQAQAERNLAQ----VTLTRQQALAKTQAISKQDLDTATTELAVKQAQIGTIDAQIKRN 170
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335

                          90
                  ....*....|..
gi 1915222241 171 QASLDTAKTNLD 182
Cdd:COG1196   336 EEELEELEEELE 347
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 88-182 2.89e-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: 39.36  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  88 LLGVIDPEQAENQIREVEATLMELRAQRAQAQAErnLAQVTLTRQQALAKTQAISKQdLDTATTELAVKQAQIGTIDAQI 167
Cdd:COG4942     9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKE--LAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*
gi 1915222241 168 KRNQASLDTAKTNLD 182
Cdd:COG4942    86 AELEKEIAELRAELE 100
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-203 3.66e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 3.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   42 RPGELQQNVL---ATGKLDALRK-----VDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIDpEQAENQI--REVEATLMEL 111
Cdd:COG4913    595 RRRIRSRYVLgfdNRAKLAALEAelaelEEELAEAEERLEALEAELDALQERREALQRLA-EYSWDEIdvASAEREIAEL 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  112 RAQRAQAQAernlAQVTLtrqQALAKTQAISKQDLDTATTELAVKQAQIGTIDAQIKRNQASLDTAKTNLDYtqivAPMA 191
Cdd:COG4913    674 EAELERLDA----SSDDL---AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA----AEDL 742

                          170
                   ....*....|..
gi 1915222241  192 GEVTQITTLQGQ 203
Cdd:COG4913    743 ARLELRALLEER 754
PycA COG1038
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ...
 35-116 7.35e-03

Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440660 [Multi-domain]  Cd Length: 1144  Bit Score: 38.52  E-value: 7.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241   35 QYRTLIVRPGELQQNVLATGKLDALRKVDVGAQVSGQLKTLSVEIGDKVKKGQLLGVIdpeqaenqirevEATLME--LR 112
Cdd:COG1038   1050 QPREVRVRDRSVKVTVASREKADPGNPGHIGAPMPGTVVKVLVKEGDEVKKGDPLLTI------------EAMKMEttIT 1117


                   ....
gi 1915222241  113 AQRA 116
Cdd:COG1038   1118 APRD 1121
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 95-181 8.68e-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: 37.82  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915222241  95 EQAENQIREVEATLMELRAQRAQAQAERNLAQVTLtrqQALAKTQAISKQDLDTATTELAVKQAQIGTIDAQIKRNQASL 174
Cdd:COG4942    23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQL---AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99


                  ....*..
gi 1915222241 175 DTAKTNL 181
Cdd:COG4942   100 EAQKEEL 106
 
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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