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Conserved domains on  [gi|2125681775|ref|WP_227413374|]
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HlyD family secretion protein [Klebsiella pneumoniae]

Protein Classification

HlyD family secretion protein( domain architecture ID 11999510)

HlyD family secretion protein similar to Escherichia coli colicin V secretion protein CvaA and microcin H47 secretion protein MchE

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-343 2.62e-44

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: 154.89  E-value: 2.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  46 SGSYTRRINVSAEVTTWPRPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSKTTRSGVVSDNEFNEITSQLHGIDEI 125
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 126 IRNLEKGRDEtLQSIKDQRNKYKEAYDISSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSLYYQQENSVLS 205
Cdd:pfam00529  81 LDRLQALESE-LAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 206 IKNQNIQNALQIKNLEREVQiqtSEYDSRIYQMKLQRNELKKELIKSGLN-SSIIIRSPSDGIIDTLNVS-QGQIVNAGD 283
Cdd:pfam00529 160 TVAQLDQIYVQITQSAAENQ---AEVRSELSGAQLQIAEAEAELKLAKLDlERTEIRAPVDGTVAFLSVTvDGGTVSAGL 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 284 TLSQIIPERDrkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKFGQFNGIIHSISKEGA 343
Cdd:pfam00529 237 RLMFVVPEDN--LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
 
Name Accession Description Interval E-value
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-343 2.62e-44

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: 154.89  E-value: 2.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  46 SGSYTRRINVSAEVTTWPRPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSKTTRSGVVSDNEFNEITSQLHGIDEI 125
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 126 IRNLEKGRDEtLQSIKDQRNKYKEAYDISSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSLYYQQENSVLS 205
Cdd:pfam00529  81 LDRLQALESE-LAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 206 IKNQNIQNALQIKNLEREVQiqtSEYDSRIYQMKLQRNELKKELIKSGLN-SSIIIRSPSDGIIDTLNVS-QGQIVNAGD 283
Cdd:pfam00529 160 TVAQLDQIYVQITQSAAENQ---AEVRSELSGAQLQIAEAEAELKLAKLDlERTEIRAPVDGTVAFLSVTvDGGTVSAGL 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 284 TLSQIIPERDrkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKFGQFNGIIHSISKEGA 343
Cdd:pfam00529 237 RLMFVVPEDN--LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
50-339 1.46e-34

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 129.01  E-value: 1.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  50 TRRINVSAEVTTwpRPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSKTTRSGVVSDNEFNEITSQLhgideiirnl 129
Cdd:COG1566    32 DEPVTADGRVEA--RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQL---------- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 130 ekgrdETLQSIKDQRNKYKEAydisSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSLYYQQENSVLSIKNQ 209
Cdd:COG1566   100 -----ARLEAELGAEAEIAAA----EAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 210 NIQNALQIKNLEREVQIQtseydSRIYQMKLQRNELKKELiksglnSSIIIRSPSDGIIDTLNVSQGQIVNAGDTLSQII 289
Cdd:COG1566   171 LAQAQAGLREEEELAAAQ-----AQVAQAEAALAQAELNL------ARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2125681775 290 PERDrkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKfgqFNGIIHSIS 339
Cdd:COG1566   240 PLDD--LWVEAYVPETDLGRVKPGQPVEVRVDAYPDRV---FEGKVTSIS 284
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 71-339 2.82e-17

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: 82.36  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  71 SQQGYVVRS-YVKEGQKIRKGDRLYELDTSKT------------------TRSGVVSD----NEFNEITSQLHG--IDEI 125
Cdd:TIGR01843  48 HLEGGIVREiLVREGDRVKAGQVLVELDATDVeadaaelesqvlrleaevARLRAEADsqaaIEFPDDLLSAEDpaVPEL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 126 I---RNLEKGRDETLQSIKDQRNkykEAYDISSSIVRTAEQGLQKMENNMRNYeqyrknglinNDQLTNQMSLYYQQ--- 199
Cdd:TIGR01843 128 IkgqQSLFESRKSTLRAQLELIL---AQIKQLEAELAGLQAQLQALRQQLEVI----------SEELEARRKLKEKGlvs 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 200 ENSVLSIKNQNIQNALQIKNLEREVQIQTSEYDSRIYQMKLQRNELKKELIK---------SGLN----------SSIII 260
Cdd:TIGR01843 195 RLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREEVLEelteaqarlAELRerlnkardrlQRLII 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 261 RSPSDGIIDTL-NVSQGQIVNAGDTLSQIIPERDRkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKFGQFNGIIHSIS 339
Cdd:TIGR01843 275 RSPVDGTVQSLkVHTVGGVVQPGETLMEIVPEDDP-LEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSIS 353
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 258-288 2.53e-03

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: 35.85  E-value: 2.53e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2125681775 258 IIIRSPSDGIIDTLNVSQGQIVNAGDTLSQI 288
Cdd:cd06850    37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 73-102 4.84e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.39  E-value: 4.84e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2125681775  73 QGYVVRSYVKEGQKIRKGDRLYELDTSKTT 102
Cdd:PRK14875   16 EGKVAGWLVQEGDEVEKGDELLDVETDKIT 45
 
Name Accession Description Interval E-value
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-343 2.62e-44

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: 154.89  E-value: 2.62e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  46 SGSYTRRINVSAEVTTWPRPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSKTTRSGVVSDNEFNEITSQLHGIDEI 125
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 126 IRNLEKGRDEtLQSIKDQRNKYKEAYDISSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSLYYQQENSVLS 205
Cdd:pfam00529  81 LDRLQALESE-LAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 206 IKNQNIQNALQIKNLEREVQiqtSEYDSRIYQMKLQRNELKKELIKSGLN-SSIIIRSPSDGIIDTLNVS-QGQIVNAGD 283
Cdd:pfam00529 160 TVAQLDQIYVQITQSAAENQ---AEVRSELSGAQLQIAEAEAELKLAKLDlERTEIRAPVDGTVAFLSVTvDGGTVSAGL 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 284 TLSQIIPERDrkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKFGQFNGIIHSISKEGA 343
Cdd:pfam00529 237 RLMFVVPEDN--LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTG 294
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
50-339 1.46e-34

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 129.01  E-value: 1.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  50 TRRINVSAEVTTwpRPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSKTTRSGVVSDNEFNEITSQLhgideiirnl 129
Cdd:COG1566    32 DEPVTADGRVEA--RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQL---------- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 130 ekgrdETLQSIKDQRNKYKEAydisSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSLYYQQENSVLSIKNQ 209
Cdd:COG1566   100 -----ARLEAELGAEAEIAAA----EAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQ 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 210 NIQNALQIKNLEREVQIQtseydSRIYQMKLQRNELKKELiksglnSSIIIRSPSDGIIDTLNVSQGQIVNAGDTLSQII 289
Cdd:COG1566   171 LAQAQAGLREEEELAAAQ-----AQVAQAEAALAQAELNL------ARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIV 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2125681775 290 PERDrkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKfgqFNGIIHSIS 339
Cdd:COG1566   240 PLDD--LWVEAYVPETDLGRVKPGQPVEVRVDAYPDRV---FEGKVTSIS 284
type_I_hlyD TIGR01843
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ...
 71-339 2.82e-17

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: 82.36  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  71 SQQGYVVRS-YVKEGQKIRKGDRLYELDTSKT------------------TRSGVVSD----NEFNEITSQLHG--IDEI 125
Cdd:TIGR01843  48 HLEGGIVREiLVREGDRVKAGQVLVELDATDVeadaaelesqvlrleaevARLRAEADsqaaIEFPDDLLSAEDpaVPEL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 126 I---RNLEKGRDETLQSIKDQRNkykEAYDISSSIVRTAEQGLQKMENNMRNYeqyrknglinNDQLTNQMSLYYQQ--- 199
Cdd:TIGR01843 128 IkgqQSLFESRKSTLRAQLELIL---AQIKQLEAELAGLQAQLQALRQQLEVI----------SEELEARRKLKEKGlvs 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 200 ENSVLSIKNQNIQNALQIKNLEREVQIQTSEYDSRIYQMKLQRNELKKELIK---------SGLN----------SSIII 260
Cdd:TIGR01843 195 RLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREEVLEelteaqarlAELRerlnkardrlQRLII 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 261 RSPSDGIIDTL-NVSQGQIVNAGDTLSQIIPERDRkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEKFGQFNGIIHSIS 339
Cdd:TIGR01843 275 RSPVDGTVQSLkVHTVGGVVQPGETLMEIVPEDDP-LEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGILNGKVKSIS 353
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 46-339 2.27e-16

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: 78.83  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  46 SGSYTRRINVSAEVTTWpRPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSKttrsgvvsdnefneitsqlhgidei 125
Cdd:COG0845     5 RGDVPETVEATGTVEAR-REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPD------------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 126 irnlekgrdetlqsikdqrnkYKEAYDISSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSLYYQQENSVls 205
Cdd:COG0845    59 ---------------------LQAALAQAQAQLAAAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAAL-- 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 206 iknQNIQNALQiknlerevqiqtseydsriyQMKLQRNELKkeliksglnssiiIRSPSDGIIDTLNVSQGQIVNAGDTL 285
Cdd:COG0845   116 ---AAAQAALE--------------------QARANLAYTT-------------IRAPFDGVVGERNVEPGQLVSAGTPL 159

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2125681775 286 SQIIpeRDRKLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEkfgQFNGIIHSIS 339
Cdd:COG0845   160 FTIA--DLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGK---TFEGKVTFID 208
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 260-324 7.14e-11

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


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 58.53  E-value: 7.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2125681775 260 IRSPSDGIIDTLNVSQGQIVNAGDTLSQIIPerDRKLYLILWIPDMAVPYIKKGDHVRIRYDAFA 324
Cdd:pfam13437   2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVP--PDRLLVEAFVPAADLGSLKKGQKVTLKLDPGS 64
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 50-339 8.38e-10

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: 59.25  E-value: 8.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775  50 TRRINVSAEVTTWPRPI---VISTSQQGYVVRSYVKEGQKIRKGDRLYELDtskttrsgvvsdnefneitsqlhgideii 126
Cdd:TIGR01730   8 SETLANTLTFPGSLEAVdeaDLAAEVAGKITKISVREGQKVKKGQVLARLD----------------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 127 rnlekgrdetlqsikdqRNKYKEAYDISSSIVRTAEQGLQKMENNMRNYEQYRKNGLINNDQLTNQMSlyyqqensvlsi 206
Cdd:TIGR01730  59 -----------------DDDYQLALQAALAQLAAAEAQLELAQRSFERAERLVKRNAVSQADLDDAKA------------ 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 207 knqniqnalQIKNLEREVQIQTSEYDSriYQMKLQRNElkkeliksglnssiiIRSPSDGIIDTLNVSQGQIVNAGDTLS 286
Cdd:TIGR01730 110 ---------AVEAAQADLEAAKASLAS--AQLNLRYTE---------------IRAPFDGTIGRRLVEVGAYVTAGQTLA 163

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2125681775 287 QIIpERDRkLYLILWIPDMAVPYIKKGDHVRIRYDAFAYEkfgQFNGIIHSIS 339
Cdd:TIGR01730 164 TIV-DLDP-LEADFSVPERDLPQLRRGQTLTVELDALPGE---EFKGKLRFID 211
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 247-328 1.31e-09

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: 57.52  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2125681775 247 KELIKSG-LNSSIIIRSPSDGIIDTLNVSQGQIVNAGDTLSQI-----------IPERDrklylilwipdmaVPYIKKGD 314
Cdd:pfam16576  97 AELERTGkVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIadlstvwveadVPEQD-------------LALVKVGQ 163

                          90
                  ....*....|....
gi 2125681775 315 HVRIRYDAFAYEKF 328
Cdd:pfam16576 164 PAEVTLPALPGKTF 177
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
64-100 2.49e-04

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 38.19  E-value: 2.49e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2125681775  64 RPIVISTSQQGYVVRSYVKEGQKIRKGDRLYELDTSK 100
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPE 37
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
257-288 4.54e-04

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 37.42  E-value: 4.54e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2125681775 257 SIIIRSPSDGIIDTLNVSQGQIVNAGDTLSQI 288
Cdd:pfam13533   2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATL 33
biotinyl_domain cd06850
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ...
 258-288 2.53e-03

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: 35.85  E-value: 2.53e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2125681775 258 IIIRSPSDGIIDTLNVSQGQIVNAGDTLSQI 288
Cdd:cd06850    37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 73-102 4.84e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.39  E-value: 4.84e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2125681775  73 QGYVVRSYVKEGQKIRKGDRLYELDTSKTT 102
Cdd:PRK14875   16 EGKVAGWLVQEGDEVEKGDELLDVETDKIT 45
 
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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