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Conserved domains on  [gi|2721285894|ref|WP_342100168|]
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HlyD family efflux transporter periplasmic adaptor subunit [Pectobacterium betavasculorum]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

CATH:  2.40.50.100|2.40.420.20|2.40.30.170|1.10.287.470
Gene Ontology:  GO:0016020|GO:0055085|GO:0022857|GO:0042802
PubMed:  32073314
TCDB:  2.A.6

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 202-427 6.91e-30

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: 118.51  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 202 PVRQSVLAPAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELENRLESARQAFATADAQYRQAQQQ--- 278
Cdd:COG0845     7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAEler 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 279 --ALFDANS---------KASLAVLQSRREQAQSDMDFLQRQQERMQLVSPRDGVAILDDASdwIGRSVAVGERIMIIAD 347
Cdd:COG0845    87 ykALLKKGAvsqqeldqaKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE--PGQLVSAGTPLFTIAD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 348 PHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIgyraAPTPDNVM-AYRLRARFTQDDPLLRVGLKGTAK 426
Cdd:COG0845   165 LDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFI----DPAVDPATrTVRVRAELPNPDGLLRPGMFVRVR 240


                  .
gi 2721285894 427 L 427
Cdd:COG0845   241 I 241
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 202-427 6.91e-30

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: 118.51  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 202 PVRQSVLAPAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELENRLESARQAFATADAQYRQAQQQ--- 278
Cdd:COG0845     7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAEler 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 279 --ALFDANS---------KASLAVLQSRREQAQSDMDFLQRQQERMQLVSPRDGVAILDDASdwIGRSVAVGERIMIIAD 347
Cdd:COG0845    87 ykALLKKGAvsqqeldqaKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE--PGQLVSAGTPLFTIAD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 348 PHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIgyraAPTPDNVM-AYRLRARFTQDDPLLRVGLKGTAK 426
Cdd:COG0845   165 LDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFI----DPAVDPATrTVRVRAELPNPDGLLRPGMFVRVR 240


                  .
gi 2721285894 427 L 427
Cdd:COG0845   241 I 241
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 201-430 1.37e-14

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: 74.27  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 201 IPVRQSVLAPAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLD--------------VRELENRLESARQAF- 265
Cdd:TIGR01730   9 ETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDdddyqlalqaalaqLAAAEAQLELAQRSFe 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 266 -ATADAQYRQAQQQALFDAnsKASLAVLQSRREQAQSDMDFLQRQQERMQLVSPRDGVaiLDDASDWIGRSVAVGERIMI 344
Cdd:TIGR01730  89 rAERLVKRNAVSQADLDDA--KAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGT--IGRRLVEVGAYVTAGQTLAT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 345 IADPHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIgyraAPTPD-NVMAYRLRARFTQDDPLLRVGLKG 423
Cdd:TIGR01730 165 IVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFI----DPRVDsGTGTVRVRATFPNPDGRLLPGMFG 240


                  ....*..
gi 2721285894 424 TAKLYGK 430
Cdd:TIGR01730 241 RVTISLK 247
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 315-420 9.67e-10

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: 55.83  E-value: 9.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 315 LVSPRDGVaiLDDASDWIGRSVAVGERIMIIADPHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIGyrA 394
Cdd:pfam13437   2 IRAPVDGV--VAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRIS--P 77

                          90       100
                  ....*....|....*....|....*...
gi 2721285894 395 APTPDNvMAYRLRARFTQD--DPLLRVG 420
Cdd:pfam13437  78 TVDPDT-GVIPVRVSIENPktPIPLLPG 104
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 221-249 4.54e-06

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 43.94  E-value: 4.54e-06
                          10        20
                  ....*....|....*....|....*....
gi 2721285894 221 VRAPVAGVVDDILVRPNQTVSANQPLVRL 249
Cdd:cd06850    39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 209-256 2.95e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 37.87  E-value: 2.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2721285894 209 APAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELEN 256
Cdd:PRK06549   52 APQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMEN 99
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 202-427 6.91e-30

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: 118.51  E-value: 6.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 202 PVRQSVLAPAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELENRLESARQAFATADAQYRQAQQQ--- 278
Cdd:COG0845     7 DVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAEler 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 279 --ALFDANS---------KASLAVLQSRREQAQSDMDFLQRQQERMQLVSPRDGVAILDDASdwIGRSVAVGERIMIIAD 347
Cdd:COG0845    87 ykALLKKGAvsqqeldqaKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE--PGQLVSAGTPLFTIAD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 348 PHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIgyraAPTPDNVM-AYRLRARFTQDDPLLRVGLKGTAK 426
Cdd:COG0845   165 LDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFI----DPAVDPATrTVRVRAELPNPDGLLRPGMFVRVR 240


                  .
gi 2721285894 427 L 427
Cdd:COG0845   241 I 241
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
179-427 1.34e-17

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 83.56  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 179 KTPPARRRLMLAAAIALVLILLIPVRQS-----VLAPAEIVAhRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRE 253
Cdd:COG1566     2 KALKKRRLLALVLLLLALGLALWAAGRNgpdepVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 254 LENRLESARQAFATADAQYRQAQQQALFDANSKASLAVLQSRR------------------------------------- 296
Cdd:COG1566    81 LQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQaqldlaqreleryqalykkgavsqqeldearaaldaa 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 297 -------------------------------EQAQSDMDFLQRQQERMQLVSPRDGVaiLDDASDWIGRSVAVGERIMII 345
Cdd:COG1566   161 qaqleaaqaqlaqaqaglreeeelaaaqaqvAQAEAALAQAELNLARTTIRAPVDGV--VTNLNVEPGEVVSAGQPLLTI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 346 ADPHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIGYRAAPTPDNVMA-------YRLRARFTQDDPL-L 417
Cdd:COG1566   239 VPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNAtgnvvqrYPVRIRLDNPDPEpL 318

                         330
                  ....*....|
gi 2721285894 418 RVGLKGTAKL 427
Cdd:COG1566   319 RPGMSATVEI 328
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 201-430 1.37e-14

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: 74.27  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 201 IPVRQSVLAPAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLD--------------VRELENRLESARQAF- 265
Cdd:TIGR01730   9 ETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDdddyqlalqaalaqLAAAEAQLELAQRSFe 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 266 -ATADAQYRQAQQQALFDAnsKASLAVLQSRREQAQSDMDFLQRQQERMQLVSPRDGVaiLDDASDWIGRSVAVGERIMI 344
Cdd:TIGR01730  89 rAERLVKRNAVSQADLDDA--KAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGT--IGRRLVEVGAYVTAGQTLAT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 345 IADPHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIgyraAPTPD-NVMAYRLRARFTQDDPLLRVGLKG 423
Cdd:TIGR01730 165 IVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFI----DPRVDsGTGTVRVRATFPNPDGRLLPGMFG 240


                  ....*..
gi 2721285894 424 TAKLYGK 430
Cdd:TIGR01730 241 RVTISLK 247
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 315-420 9.67e-10

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: 55.83  E-value: 9.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 315 LVSPRDGVaiLDDASDWIGRSVAVGERIMIIADPHDVELEIQLPAADAIALENGADVRLFLNVAPNSAQEARLEQIGyrA 394
Cdd:pfam13437   2 IRAPVDGV--VAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRIS--P 77

                          90       100
                  ....*....|....*....|....*...
gi 2721285894 395 APTPDNvMAYRLRARFTQD--DPLLRVG 420
Cdd:pfam13437  78 TVDPDT-GVIPVRVSIENPktPIPLLPG 104
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 200-398 4.02e-08

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: 54.74  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 200 LIPVRQSVLAPAEIVAHR-PVMVRAPVAGVVDDILVRPNQTVSANQPLVRLD-------VRELENRLESARQAFATADAQ 271
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGnAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDptdyqaaLDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 272 YRQAQQQALFDANSKASLAVLQSRRE-------QAQSDMDFLQRQQERMQLVSPRDGVAI--LDDAsdwiGRSVAVGE-- 340
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRaaqaavkAAQAQLAQAQIDLARRRVLAPIGGISResLVTA----GALVAQAQan 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2721285894 341 RIMIIADPHDVELEIQLPAADAIALENGADVRLFLNVApnsAQEARLEQIGYRAAPTP 398
Cdd:pfam00529 157 LLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIA---EAEAELKLAKLDLERTE 211
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 221-249 4.54e-06

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 43.94  E-value: 4.54e-06
                          10        20
                  ....*....|....*....|....*....
gi 2721285894 221 VRAPVAGVVDDILVRPNQTVSANQPLVRL 249
Cdd:cd06850    39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
217-266 1.12e-04

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 39.73  E-value: 1.12e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2721285894 217 RPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELENRLESARQAFA 266
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 221-262 1.35e-04

The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.


Pssm-ID: 133459 [Multi-domain]  Cd Length: 67  Bit Score: 39.71  E-value: 1.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2721285894 221 VRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELENRLESAR 262
Cdd:cd06850     2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEVTAPV 43
AccB COG0511
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ...
 221-250 1.67e-04

Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440277 [Multi-domain]  Cd Length: 136  Bit Score: 41.42  E-value: 1.67e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2721285894 221 VRAPVAGVVDDILVRPNQTVSANQPLVRLD 250
Cdd:COG0511   107 IEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 221-390 6.55e-04

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: 40.95  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 221 VRAPVAGVVDDILVR-PNQTVSANQPLVRLDVRElenrLESARQAFATADAQYRQAQQQALFDAnSKASLAVLQSRREQA 299
Cdd:pfam16576  22 VHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPE----LVAAQQEYLLALRSGDALSKSELLRA-ARQRLRLLGMPEAQI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2721285894 300 QSdmdfLQRQ---QERMQLVSPRDGVAILDDASDwiGRSVAVGERIMIIADPHDVELEIQLPAADAIALENGADVRLFLN 376
Cdd:pfam16576  97 AE----LERTgkvQPTVTVYAPISGVVTELNVRE--GMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLP 170

                         170
                  ....*....|....
gi 2721285894 377 VAPNSAQEARLEQI 390
Cdd:pfam16576 171 ALPGKTFEGKVDYI 184
PRK06549 PRK06549
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
 209-256 2.95e-03

acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated


Pssm-ID: 235826 [Multi-domain]  Cd Length: 130  Bit Score: 37.87  E-value: 2.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2721285894 209 APAEIVAHRPVMVRAPVAGVVDDILVRPNQTVSANQPLVRLDVRELEN 256
Cdd:PRK06549   52 APQPAAAAGADAMPSPMPGTILKVLVAVGDQVTENQPLLILEAMKMEN 99
 
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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