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Conserved domains on  [gi|736906489|ref|WP_034905048|]
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F0F1 ATP synthase subunit B [Campylobacter sp. MIT 97-5078]

Protein Classification

F0F1 ATP synthase subunit B( domain architecture ID 10793096)

F0F1 ATP synthase subunit B is part of the membrane proton channel of the F-type ATPase that produces ATP from ADP in the presence of a proton gradient across the membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 3-167 3.95e-54

F0F1 ATP synthase subunit B; Validated


:

Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 168.65  E-value: 3.95e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489   3 KIGFVLAFLPLALFAAPNGSGEYDIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETI 82
Cdd:PRK08475   1 KFFFLLLLGFYAFAASLGATEQYDIIERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  83 KKLEDAKKEAIVAINTAKKEAELLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKILNQMFSE--CKLKQDEIL 160
Cdd:PRK08475  81 KKLEEAKEKAELIVETAKKEAYILTQKIEKQTKDDIENLIKSFEELMEFEVRKMEREVVEEVLNELFESkkVSLNQQEYV 160


                 ....*..
gi 736906489 161 DIMLKKV 167
Cdd:PRK08475 161 NILLKKV 167
 
Name Accession Description Interval E-value
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 3-167 3.95e-54

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 168.65  E-value: 3.95e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489   3 KIGFVLAFLPLALFAAPNGSGEYDIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETI 82
Cdd:PRK08475   1 KFFFLLLLGFYAFAASLGATEQYDIIERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  83 KKLEDAKKEAIVAINTAKKEAELLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKILNQMFSE--CKLKQDEIL 160
Cdd:PRK08475  81 KKLEEAKEKAELIVETAKKEAYILTQKIEKQTKDDIENLIKSFEELMEFEVRKMEREVVEEVLNELFESkkVSLNQQEYV 160


                 ....*..
gi 736906489 161 DIMLKKV 167
Cdd:PRK08475 161 NILLKKV 167
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 26-140 1.29e-10

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: 55.91  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  26 DIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAEL 105
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 736906489 106 LAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEV 140
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAEL 115
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 25-144 5.40e-10

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: 54.79  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  25 YDIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAE 104
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 736906489 105 LLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKI 144
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV 120
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 31-133 2.76e-05

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 41.53  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489   31 TINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAELLAVKL 110
Cdd:pfam00430   6 LIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEI 85

                          90       100
                  ....*....|....*....|...
gi 736906489  111 KNDTKNDIALLEKHFEEQKVYEQ 133
Cdd:pfam00430  86 VAAAEAEAERIIEQAAAEIEQEK 108
 
Name Accession Description Interval E-value
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 3-167 3.95e-54

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 168.65  E-value: 3.95e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489   3 KIGFVLAFLPLALFAAPNGSGEYDIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETI 82
Cdd:PRK08475   1 KFFFLLLLGFYAFAASLGATEQYDIIERTINFLIFVGILWYFAAKPLKNFYKSRINKISKRLEEIQEKLKESKEKKEDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  83 KKLEDAKKEAIVAINTAKKEAELLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKILNQMFSE--CKLKQDEIL 160
Cdd:PRK08475  81 KKLEEAKEKAELIVETAKKEAYILTQKIEKQTKDDIENLIKSFEELMEFEVRKMEREVVEEVLNELFESkkVSLNQQEYV 160


                 ....*..
gi 736906489 161 DIMLKKV 167
Cdd:PRK08475 161 NILLKKV 167
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 26-140 1.29e-10

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: 55.91  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  26 DIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAEL 105
Cdd:cd06503    1 TLIWQIINFLILLFILKKFLWKPILKALDEREEKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEK 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 736906489 106 LAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEV 140
Cdd:cd06503   81 IKEEILAEAKEEAERILEQAKAEIEQEKEKALAEL 115
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 25-144 5.40e-10

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: 54.79  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  25 YDIIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAE 104
Cdd:COG0711    1 GTLFWQLINFLILVLLLKKFAWPPILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAE 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 736906489 105 LLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKI 144
Cdd:COG0711   81 AIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEV 120
atpF CHL00019
ATP synthase CF0 B subunit
 32-137 2.02e-05

ATP synthase CF0 B subunit


Pssm-ID: 176962 [Multi-domain]  Cd Length: 184  Bit Score: 42.54  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  32 INFLIFVAILFYFLARPAKEFYNNRITKIatrLEEIQN--KVLESKNKKLETIKK-LEDAKKEAIVAINTAKKEAELLAV 108
Cdd:CHL00019  32 INLSVVLGVLIYFGKGVLSDLLDNRKQTI---LNTIRNseERREEAIEKLEKARArLRQAELEADEIRVNGYSEIEREKE 108

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 736906489 109 KLKNDTKNDIALLEK------HFEEQKVYEQRKMQ 137
Cdd:CHL00019 109 NLINQAKEDLERLENyknetiRFEQQRAINQVRQQ 143
ATP-synt_B pfam00430
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ...
 31-133 2.76e-05

ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006


Pssm-ID: 425677 [Multi-domain]  Cd Length: 132  Bit Score: 41.53  E-value: 2.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489   31 TINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAELLAVKL 110
Cdd:pfam00430   6 LIAFLILVGVLIKFAWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEIIENAKKRAEKLKEEI 85

                          90       100
                  ....*....|....*....|...
gi 736906489  111 KNDTKNDIALLEKHFEEQKVYEQ 133
Cdd:pfam00430  86 VAAAEAEAERIIEQAAAEIEQEK 108
PTZ00121 PTZ00121
MAEBL; Provisional
 61-159 2.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 37.81  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489   61 ATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVaintAKKEAELLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEV 140
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA----AKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389

                          90       100
                  ....*....|....*....|.
gi 736906489  141 IAKI--LNQMFSECKLKQDEI 159
Cdd:PTZ00121 1390 KKKAdeAKKKAEEDKKKADEL 1410
PRK14474 PRK14474
F0F1 ATP synthase subunit B; Provisional
 27-148 4.99e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184696 [Multi-domain]  Cd Length: 250  Bit Score: 36.33  E-value: 4.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  27 IIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLE--DAKKEAIVAinTAKKEAE 104
Cdd:PRK14474   8 VVAQIINFLILVYLLRRFLYKPIIQVMKKRQQRIANRWQDAEQRQQEAGQEAERYRQKQQslEQQRASFMA--QAQEAAD 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 736906489 105 LLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKILNQM 148
Cdd:PRK14474  86 EQRQHLLNEAREDVATARDEWLEQLEREKQEFFKALQQQTGQQM 129
PRK13455 PRK13455
F0F1 ATP synthase subunit B; Provisional
 31-140 5.27e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184062 [Multi-domain]  Cd Length: 184  Bit Score: 35.93  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  31 TINFLIFVAILFYF-LARPAKEFYNNRITKIATRLEEIQ------NKVLESKNKKLETIKkledAKKEAIVAinTAKKEA 103
Cdd:PRK13455  33 TLAFLLFIGILVYFkVPGMIGGMLDKRAEGIRSELEEARalreeaQTLLASYERKQREVQ----EQADRIVA--AAKDEA 106

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 736906489 104 ELLAVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEV 140
Cdd:PRK13455 107 QAAAEQAKADLEASIARRLAAAEDQIASAEAAAVKAV 143
PRK14473 PRK14473
F0F1 ATP synthase subunit B; Provisional
 27-144 6.43e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 172948 [Multi-domain]  Cd Length: 164  Bit Score: 35.28  E-value: 6.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736906489  27 IIPRTINFLIFVAILFYFLARPAKEFYNNRITKIATRLEEIQNKVLESKNKKLETIKKLEDAKKEAIVAINTAKKEAELL 106
Cdd:PRK14473  11 LIAQLINFLLLIFLLRTFLYRPVLNLLNERTRRIEESLRDAEKVREQLANAKRDYEAELAKARQEAAKIVAQAQERARAQ 90

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 736906489 107 AVKLKNDTKNDIALLEKHFEEQKVYEQRKMQKEVIAKI 144
Cdd:PRK14473  91 EAEIIAQARREAEKIKEEARAQAEQERQRMLSELKSQI 128
 
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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