Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5F4Z4 (ATPF_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:NGO2146
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [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_0000368619

Regions

Transmembrane7 – 2721Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q5F4Z4 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 6DE2BAC3C57874C5

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

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

       130        140        150 
RDQVAVLAVK GAESILRSEV DASKHAKLLD TLKQEL 

« Hide

References

[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004969 Genomic DNA. Translation: AAW90743.1.
RefSeqYP_209155.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ5F4Z4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242231.NGO2146.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW90743; AAW90743; NGO2146.
GeneID3282775.
KEGGngo:NGO2146.
PATRIC20338145. VBINeiGon24812_2595.

Phylogenomic databases

eggNOGCOG0711.
HOGENOMHOG000015378.
KOK02109.
OMALIFWTAV.
OrthoDBEOG6DNTDK.

Enzyme and pathway databases

BioCycNGON242231:GI2G-2037-MONOMER.

Family and domain databases

Gene3D1.20.5.620. 1 hit.
HAMAPMF_01398. ATP_synth_b_bact.
InterProIPR028987. ATPase_B-like_membr.
IPR002146. ATPase_F0-cplx_b/b'su_bac.
IPR005864. ATPase_F0-cplx_bsu_bac.
[Graphical view]
PfamPF00430. ATP-synt_B. 1 hit.
[Graphical view]
SUPFAMSSF81573. SSF81573. 1 hit.
TIGRFAMsTIGR01144. ATP_synt_b. 1 hit.
ProtoNetSearch...

Entry information

Entry nameATPF_NEIG1
AccessionPrimary (citable) accession number: Q5F4Z4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 15, 2005
Last modified: June 11, 2014
This is version 58 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