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B4RJF6

- ATPF_NEIG2

UniProt

B4RJF6 - ATPF_NEIG2

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Protein

ATP synthase subunit b

Gene

atpF

Organism
Neisseria gonorrhoeae (strain NCCP11945)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation.UniRule annotation
Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0.UniRule annotation

GO - Molecular functioni

  1. proton-transporting ATP synthase activity, rotational mechanism Source: UniProtKB-HAMAP

GO - Biological processi

  1. plasma membrane ATP synthesis coupled proton transport Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciNGON521006:GJ73-2695-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit bUniRule annotation
Alternative name(s):
ATP synthase F(0) sector subunit bUniRule annotation
ATPase subunit IUniRule annotation
F-type ATPase subunit bUniRule annotation
Short name:
F-ATPase subunit bUniRule annotation
Gene namesi
Name:atpFUniRule annotation
Ordered Locus Names:NGK_2622
OrganismiNeisseria gonorrhoeae (strain NCCP11945)
Taxonomic identifieri521006 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002564: Chromosome

Subcellular locationi

Cell inner membrane UniRule annotation; Single-pass membrane protein UniRule annotation

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-HAMAP
  3. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, CF(0), Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156ATP synthase subunit bPRO_0000368620Add
BLAST

Interactioni

Subunit structurei

F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains.UniRule annotation

Protein-protein interaction databases

STRINGi521006.NGK_2622.

Structurei

3D structure databases

ProteinModelPortaliB4RJF6.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2721HelicalUniRule annotationAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase B chain family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0711.
HOGENOMiHOG000015378.
KOiK02109.
OMAiLIFWTAV.
OrthoDBiEOG6DNTDK.

Family and domain databases

Gene3Di1.20.5.620. 1 hit.
HAMAPiMF_01398. ATP_synth_b_bact.
InterProiIPR028987. ATPase_B-like_membr.
IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]
PfamiPF00430. ATP-synt_B. 1 hit.
[Graphical view]
SUPFAMiSSF81573. SSF81573. 1 hit.
TIGRFAMsiTIGR01144. ATP_synt_b. 1 hit.

Sequencei

Sequence statusi: Complete.

B4RJF6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNINATLFAQ IIVFFGLVWF TMKFVWPPIA KALDERAAKI AEGLAAAERG
60 70 80 90 100
KSDFEQAEKK VAELLAEGRN QVSEMVANAE KRAAKIVEEA KEQASSEAAR
110 120 130 140 150
IAAQAKADVE QELFRARESL RDQVAVLAVK GAESILRSEV DASKHAKLLD

TLKQEL
Length:156
Mass (Da):17,139
Last modified:September 23, 2008 - v1
Checksum:i6DE2BAC3C57874C5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001050 Genomic DNA. Translation: ACF31221.1.
RefSeqiYP_002003247.1. NC_011035.1.

Genome annotation databases

EnsemblBacteriaiACF31221; ACF31221; NGK_2622.
GeneIDi6448057.
KEGGingk:NGK_2622.
PATRICi20344023. VBINeiGon87511_2839.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001050 Genomic DNA. Translation: ACF31221.1 .
RefSeqi YP_002003247.1. NC_011035.1.

3D structure databases

ProteinModelPortali B4RJF6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 521006.NGK_2622.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACF31221 ; ACF31221 ; NGK_2622 .
GeneIDi 6448057.
KEGGi ngk:NGK_2622.
PATRICi 20344023. VBINeiGon87511_2839.

Phylogenomic databases

eggNOGi COG0711.
HOGENOMi HOG000015378.
KOi K02109.
OMAi LIFWTAV.
OrthoDBi EOG6DNTDK.

Enzyme and pathway databases

BioCyci NGON521006:GJ73-2695-MONOMER.

Family and domain databases

Gene3Di 1.20.5.620. 1 hit.
HAMAPi MF_01398. ATP_synth_b_bact.
InterProi IPR028987. ATPase_B-like_membr.
IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view ]
Pfami PF00430. ATP-synt_B. 1 hit.
[Graphical view ]
SUPFAMi SSF81573. SSF81573. 1 hit.
TIGRFAMsi TIGR01144. ATP_synt_b. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence of Neisseria gonorrhoeae NCCP11945."
    Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.
    J. Bacteriol. 190:6035-6036(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCCP11945.

Entry informationi

Entry nameiATPF_NEIG2
AccessioniPrimary (citable) accession number: B4RJF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: October 29, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3