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Q7DD66 (ATPF_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP synthase subunit b
Alternative name(s):
ATP synthase F(0) sector subunit b
ATPase subunit I
F-type ATPase subunit b
Short name=F-ATPase subunit b
Gene names
Name:atpF
Ordered Locus Names:NMB1938
OrganismNeisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]
Taxonomic identifier122586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01398

Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP-Rule MF_01398

Subunit structure

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 By similarity.

Subcellular location

Cell inner membrane; Single-pass membrane protein By similarity HAMAP-Rule MF_01398.

Sequence similarities

Belongs to the ATPase B chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 156156ATP synthase subunit b HAMAP-Rule MF_01398
PRO_0000368622

Regions

Transmembrane7 – 2721Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q7DD66 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 3DE2A468D7D4121E

FASTA15617,139
        10         20         30         40         50         60 
MNINATLFAQ IIVFFGLVWF TMKFVWPPIA KALDERAAKV AEGLAAAERG KSDFEQAEKK 

        70         80         90        100        110        120 
VAELLAEGRN QVSEMVANAE KRAAKIVEEA KEQASSEAAR IAAQAKADVE QELFRARESL 

       130        140        150 
REQVAVLAVK GAESILRSEV DASKHAKLLD TLKQEL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE002098 Genomic DNA. Translation: AAF42267.1.
PIRC81025.
RefSeqNP_274932.1. NC_003112.2.

3D structure databases

ProteinModelPortalQ7DD66.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122586.NMB1938.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF42267; AAF42267; NMB1938.
GeneID904214.
KEGGnme:NMB1938.
PATRIC20359923. VBINeiMen85645_2466.

Phylogenomic databases

eggNOGCOG0711.
HOGENOMHOG000015378.
KOK02109.
OMARKEVNAG.
OrthoDBEOG6DNTDK.
ProtClustDBPRK05759.

Enzyme and pathway databases

BioCycNMEN122586:GHGG-1995-MONOMER.

Family and domain databases

HAMAPMF_01398. ATP_synth_b_bact.
InterProIPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]
PfamPF00430. ATP-synt_B. 1 hit.
[Graphical view]
TIGRFAMsTIGR01144. ATP_synt_b. 1 hit.
ProtoNetSearch...

Entry information

Entry nameATPF_NEIMB
AccessionPrimary (citable) accession number: Q7DD66
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families