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Conserved domains on  [gi|488946648|ref|WP_002857723|]
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MULTISPECIES: FoF1 ATP synthase subunit B' [Campylobacter]

Protein Classification

FoF1 ATP synthase subunit B'( domain architecture ID 10013077)

FoF1 ATP synthase subunit B' is part of the Fo membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane; a diverged and duplicated form of B found in plants and photosynthetic bacteria

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 1-141 6.73e-50

F0F1 ATP synthase subunit B'; Validated


:

Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 156.00  E-value: 6.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   1 MFEDMHPSIMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQ 80
Cdd:PRK08476   1 MMLDVNPYLMLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488946648  81 SAIAAAKEEAEQILRSKKEELERKMASFYADLAVQKKELQEHLNIHLPELKQALQNNIKKI 141
Cdd:PRK08476  81 KAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQMPEFKEALNAKLSKI 141
 
Name Accession Description Interval E-value
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 1-141 6.73e-50

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 156.00  E-value: 6.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   1 MFEDMHPSIMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQ 80
Cdd:PRK08476   1 MMLDVNPYLMLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488946648  81 SAIAAAKEEAEQILRSKKEELERKMASFYADLAVQKKELQEHLNIHLPELKQALQNNIKKI 141
Cdd:PRK08476  81 KAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQMPEFKEALNAKLSKI 141
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 9-123 3.47e-08

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 48.97  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   9 IMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQSAIAAAKE 88
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488946648  89 EAEQILRSKKEELERKMASFYADLAVQKKELQEHL 123
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAEL 115
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 8-123 1.41e-06

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 44.78  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   8 SIMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQSAIAAAK 87
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488946648  88 EEAEQILRSKKEELERKMASFYADLAVQKKELQEHL 123
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAEL 116
 
Name Accession Description Interval E-value
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 1-141 6.73e-50

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 156.00  E-value: 6.73e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   1 MFEDMHPSIMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQ 80
Cdd:PRK08476   1 MMLDVNPYLMLATFVVFLLLIVILNSWLYKPLLKFMDNRNASIKNDLEKVKTNSSDVSEIEHEIETILKNAREEANKIRQ 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488946648  81 SAIAAAKEEAEQILRSKKEELERKMASFYADLAVQKKELQEHLNIHLPELKQALQNNIKKI 141
Cdd:PRK08476  81 KAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQELKEQLLSQMPEFKEALNAKLSKI 141
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 9-123 3.47e-08

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 48.97  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   9 IMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQSAIAAAKE 88
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488946648  89 EAEQILRSKKEELERKMASFYADLAVQKKELQEHL 123
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAEL 115
PRK07353 PRK07353
F0F1 ATP synthase subunit B'; Validated
 11-78 1.00e-06

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 235999 [Multi-domain]  Cd Length: 140  Bit Score: 44.99  E-value: 1.00e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488946648  11 LATMAI-FLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKI 78
Cdd:PRK07353   8 LPLMAVqFVLLTFILNALFYKPVGKVVEEREDYIRTNRAEAKERLAEAEKLEAQYEQQLASARKQAQAV 76
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 8-123 1.41e-06

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 44.78  E-value: 1.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488946648   8 SIMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKIKQSAIAAAK 87
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488946648  88 EEAEQILRSKKEELERKMASFYADLAVQKKELQEHL 123
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAEL 116
PRK13460 PRK13460
F0F1 ATP synthase subunit B; Provisional
 4-78 7.82e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 139585 [Multi-domain]  Cd Length: 173  Bit Score: 35.00  E-value: 7.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488946648   4 DMHPSIMLATMAIFLAMIVILNSMLYKPLLKFMDERNDSIKNDENKVKENSQEVLGVNDELEAIHINTREEIQKI 78
Cdd:PRK13460  13 DVNPGLVVWTLVTFLVVVLVLKKFAWDVILKALDERASGVQNDINKASELRLEAEALLKDYEARLNSAKDEANAI 87
 
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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