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Conserved domains on  [gi|446536477|ref|WP_000613823|]
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MULTISPECIES: metal ABC transporter permease [Bacillus]

Protein Classification

metal ABC transporter permease( domain architecture ID 11437853)

metal ABC transporter permease is the transmembrane subunit (TM) of a Periplasmic Binding Protein (PBP)-dependent ABC transporter complex that facilitates the ABC transport of specific metal ions such as manganese or zinc

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
8-275 2.00e-74

ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism];


:

Pssm-ID: 440725  Cd Length: 260  Bit Score: 228.01  E-value: 2.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477   8 YDFLRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEktiftggfLNPLYMGMIFSIGGALLIEK 87
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG--------LSPLLGALVAGLLAALLIGL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  88 LRTVYKHYQELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLSF 167
Cdd:COG1108   73 LRRRSRLKEDTAIGIVFSGGFALGVLLISLVPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 168 DEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFASY 247
Cdd:COG1108  153 DPELARASGLPVRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSY 232
                        250       260
                 ....*....|....*....|....*...
gi 446536477 248 QLDLAPGGTIVMIAVLILIGAILWKKKK 275
Cdd:COG1108  233 YLDLPTGPTIVLVAGLLFLLSLLFSPRR 260
 
Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
8-275 2.00e-74

ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism];


Pssm-ID: 440725  Cd Length: 260  Bit Score: 228.01  E-value: 2.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477   8 YDFLRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEktiftggfLNPLYMGMIFSIGGALLIEK 87
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG--------LSPLLGALVAGLLAALLIGL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  88 LRTVYKHYQELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLSF 167
Cdd:COG1108   73 LRRRSRLKEDTAIGIVFSGGFALGVLLISLVPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 168 DEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFASY 247
Cdd:COG1108  153 DPELARASGLPVRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSY 232
                        250       260
                 ....*....|....*....|....*...
gi 446536477 248 QLDLAPGGTIVMIAVLILIGAILWKKKK 275
Cdd:COG1108  233 YLDLPTGPTIVLVAGLLFLLSLLFSPRR 260
ABC-3 pfam00950
ABC 3 transport family;
7-270 1.66e-49

ABC 3 transport family;


Pssm-ID: 334323  Cd Length: 258  Bit Score: 163.94  E-value: 1.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477    7 QYDFLRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEKTIFTGGFLnplymgmiFSIGGALLIE 86
Cdd:pfam00950   1 QYEFMQRALLASILVSLACGILGSFLVLRRQSLMGDALSHAALPGVALAYFLGINPAIGAFV--------FGLIAAVAMG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477   87 KLRTVYKHYQELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLS 166
Cdd:pfam00950  73 YLKRKTRLKEDTAIGIVFSTFLALGLVLISLIPGSAVDLDSYLFGNILTISQQDLIQIAIITAVILILLLLFWKELLLIT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  167 FDEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFAS 246
Cdd:pfam00950 153 FDPDHAKVIGLPVQFLYLLLLALIALTIVVALQAVGAILVIALLIIPAATARRLTRSFDSMLIIAILIGMVSCVAGLYLS 232
                         250       260
                  ....*....|....*....|....
gi 446536477  247 YQLDLAPGGTIVMIAVLILIGAIL 270
Cdd:pfam00950 233 YYFDTSTGPVIVLIATLLFLISLA 256
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
11-266 4.24e-27

Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy.


Pssm-ID: 119348 [Multi-domain]  Cd Length: 261  Bit Score: 105.72  E-value: 4.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  11 LRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLlektiFTGGFLNPLYMGMIFSIGGALLIEKLRT 90
Cdd:cd06550    1 LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALL-----LGIGLSNYALGAFAFAGALAIALLVLLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  91 VYKH----YQELAIPIILSAGMGIGVIFISL-ANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLL 165
Cdd:cd06550   76 ASRGglspSKLILIGIVLSAFFSAGVILISLlSDDSLQDLNIWLFGSILGVTWEDLLILLIILLLVLLLLLLLSRKLNLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 166 SFDEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTlPVAASIRIANGFKQTIFFSILFGEIAVIGGMFA 245
Cdd:cd06550  156 TFDEDLAKSLGINVNLLRLLLLLLVALLVVAAVALVGVILFVGLIA-PHLARRLFGRSHRYLLPLSALLGAILLLLGDLL 234
                        250       260
                 ....*....|....*....|....
gi 446536477 246 SYQL---DLAPGGTIVMIAVLILI 266
Cdd:cd06550  235 SRTLlpsELPVGPVTALLGAPYFL 258
znuB PRK09543
zinc ABC transporter permease subunit ZnuB;
17-274 1.38e-22

zinc ABC transporter permease subunit ZnuB;


Pssm-ID: 181938  Cd Length: 261  Bit Score: 93.60  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  17 AGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEktiftggfLNPLYMGMIFSIGGALLIEKLRTVYKHYQ 96
Cdd:PRK09543  11 AGIMLACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLD--------VNPFYAVIAVTLLLAGGLVWLEKRPQLAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  97 ELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLSFDEEYAVSTG 176
Cdd:PRK09543  83 DTLLGIMAHSALSLGLVVVSLMSNVRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAILFWQWRNLLSMTISPDLAFVDG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 177 LSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFASYQLDLAPGGT 256
Cdd:PRK09543 163 VKLQRVKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPS 242
                        250
                 ....*....|....*...
gi 446536477 257 IVMIAVLILIGAILWKKK 274
Cdd:PRK09543 243 VVLCAALLFILSMMKKQA 260
 
Name Accession Description Interval E-value
ZnuB COG1108
ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and ...
8-275 2.00e-74

ABC-type Mn2+/Zn2+ transport system, permease component [Inorganic ion transport and metabolism];


Pssm-ID: 440725  Cd Length: 260  Bit Score: 228.01  E-value: 2.00e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477   8 YDFLRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEktiftggfLNPLYMGMIFSIGGALLIEK 87
Cdd:COG1108    1 YDFMQRALLAGLLVGLACGLLGVFLVLRRMSLIGDALSHAALPGVALAFLLG--------LSPLLGALVAGLLAALLIGL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  88 LRTVYKHYQELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLSF 167
Cdd:COG1108   73 LRRRSRLKEDTAIGIVFSGGFALGVLLISLVPGSAVDLMSYLFGSILAVSRSDLLLLAVLAAVVLLLLLLFYRELLLVSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 168 DEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFASY 247
Cdd:COG1108  153 DPELARASGLPVRLLHLLLLVLLALTVVAALQAVGALLVSALLIIPAATARLLTRSLRRMLLLAVLIGVLSSVLGLYLSY 232
                        250       260
                 ....*....|....*....|....*...
gi 446536477 248 QLDLAPGGTIVMIAVLILIGAILWKKKK 275
Cdd:COG1108  233 YLDLPTGPTIVLVAGLLFLLSLLFSPRR 260
ABC-3 pfam00950
ABC 3 transport family;
7-270 1.66e-49

ABC 3 transport family;


Pssm-ID: 334323  Cd Length: 258  Bit Score: 163.94  E-value: 1.66e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477    7 QYDFLRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEKTIFTGGFLnplymgmiFSIGGALLIE 86
Cdd:pfam00950   1 QYEFMQRALLASILVSLACGILGSFLVLRRQSLMGDALSHAALPGVALAYFLGINPAIGAFV--------FGLIAAVAMG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477   87 KLRTVYKHYQELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLS 166
Cdd:pfam00950  73 YLKRKTRLKEDTAIGIVFSTFLALGLVLISLIPGSAVDLDSYLFGNILTISQQDLIQIAIITAVILILLLLFWKELLLIT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  167 FDEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFAS 246
Cdd:pfam00950 153 FDPDHAKVIGLPVQFLYLLLLALIALTIVVALQAVGAILVIALLIIPAATARRLTRSFDSMLIIAILIGMVSCVAGLYLS 232
                         250       260
                  ....*....|....*....|....
gi 446536477  247 YQLDLAPGGTIVMIAVLILIGAIL 270
Cdd:pfam00950 233 YYFDTSTGPVIVLIATLLFLISLA 256
TM_ABC_iron-siderophores_like cd06550
Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding ...
11-266 4.24e-27

Transmembrane subunit (TM), of Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters involved in the uptake of siderophores, heme, vitamin B12, or the divalent cations Mg2+ and Zn2+. PBP-dependent ABC transporters consist of a PBP, two TMs, and two cytoplasmic ABCs, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The TMs are bundles of alpha helices that transverse the cytoplasmic membrane multiple times. The two ABCs bind and hydrolyze ATP and drive the transport reaction. Each TM has a prominent cytoplasmic loop which contacts an ABC and represents a conserved motif. The two TMs form either a homodimer (e.g. in the case of the BtuC subunits of the Escherichia coli BtuCD vitamin B12 transporter), a heterodimer (e.g. the TroC and TroD subunits of the Treponema pallidum general transition metal transporter, TroBCD), or a pseudo-heterodimer (e.g. the FhuB protein of the E. coli ferrichrome transporter, FhuBC). FhuB contains two tandem TMs which associate to form the pseudo-heterodimer. Both FhuB TMs are found in this hierarchy.


Pssm-ID: 119348 [Multi-domain]  Cd Length: 261  Bit Score: 105.72  E-value: 4.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  11 LRNSLYAGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLlektiFTGGFLNPLYMGMIFSIGGALLIEKLRT 90
Cdd:cd06550    1 LLAALLVGAALAVSGAILQSLTRNRLASPSILGISHGALLGVVLALL-----LGIGLSNYALGAFAFAGALAIALLVLLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  91 VYKH----YQELAIPIILSAGMGIGVIFISL-ANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLL 165
Cdd:cd06550   76 ASRGglspSKLILIGIVLSAFFSAGVILISLlSDDSLQDLNIWLFGSILGVTWEDLLILLIILLLVLLLLLLLSRKLNLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 166 SFDEEYAVSTGLSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTlPVAASIRIANGFKQTIFFSILFGEIAVIGGMFA 245
Cdd:cd06550  156 TFDEDLAKSLGINVNLLRLLLLLLVALLVVAAVALVGVILFVGLIA-PHLARRLFGRSHRYLLPLSALLGAILLLLGDLL 234
                        250       260
                 ....*....|....*....|....
gi 446536477 246 SYQL---DLAPGGTIVMIAVLILI 266
Cdd:cd06550  235 SRTLlpsELPVGPVTALLGAPYFL 258
znuB PRK09543
zinc ABC transporter permease subunit ZnuB;
17-274 1.38e-22

zinc ABC transporter permease subunit ZnuB;


Pssm-ID: 181938  Cd Length: 261  Bit Score: 93.60  E-value: 1.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  17 AGILIGLVAPLIGVFVVIRRMSLIADALSHVTLSGIAASLLLEktiftggfLNPLYMGMIFSIGGALLIEKLRTVYKHYQ 96
Cdd:PRK09543  11 AGIMLACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLD--------VNPFYAVIAVTLLLAGGLVWLEKRPQLAI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477  97 ELAIPIILSAGMGIGVIFISLANGFNTDLFSYLFGSVSAVTSTDLIIIGIVAIVVIVTITLLYKELFLLSFDEEYAVSTG 176
Cdd:PRK09543  83 DTLLGIMAHSALSLGLVVVSLMSNVRVDLMAYLFGDLLAVTPEDLISIAIGVVIVLAILFWQWRNLLSMTISPDLAFVDG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446536477 177 LSAKWIHFIFIILVALVIAVSMRVVGVLLVSSLMTLPVAASIRIANGFKQTIFFSILFGEIAVIGGMFASYQLDLAPGGT 256
Cdd:PRK09543 163 VKLQRVKLLLMLVTALTIGVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMLAVTGGLTFSAFYDTPAGPS 242
                        250
                 ....*....|....*...
gi 446536477 257 IVMIAVLILIGAILWKKK 274
Cdd:PRK09543 243 VVLCAALLFILSMMKKQA 260
 
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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