P56086 (ATPF_HELPY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	HP_1136

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Protein existence	Inferred 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 MF_01398 Component of the F0 channel, it forms part of the peripheral stalk, linking F1 to F0 By similarity. HAMAP 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 MF_01398.
Sequence similarities	Belongs to the ATPase B chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(0) Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell proton-transporting ATP synthase complex, coupling factor F(o) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 171	171	ATP synthase subunit b HAMAP MF_01398		PRO_0000082376
Regions
	Transmembrane	2 – 22	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	P56086 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: CBDBE6C8591329B2	FASTA	171	19,861
	10 20 30 40 50 60 MFVVKMVLGF LILLSPLCAT GLDISQTDII ERSLNFLLFV GILWYFSAKK LRSFLRSKSL 70 80 90 100 110 120 EISKRLEEIQ AQLKVSKENK KKLLKELEQA KEKAELIVSD ANKEAYMITQ KYELQTKMDV 130 140 150 160 170 ENLIKNSKAL MDLEVKKIKR ELVESVFKDL RESKKVSFNA QDCVNILKQR L

References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD08178.1.
PIR	H64661.
RefSeq	NP_207927.1. NC_000915.1.
3D structure databases
ProteinModelPortal	P56086.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	899673.
GenomeReviews	Gene locus HP_1136 in contig AE000511_GR.
KEGG	hpy:HP1136.
NMPDR	fig|85962.1.peg.1123.
PATRIC	20593617. VBIHelPyl33062_1188.
TIGR	HP_1136.
Phylogenomic databases
HOGENOM	HBG578849.
OMA	CVNILKQ.
ProtClustDB	PRK08475.
Family and domain databases
HAMAP	MF_01398. ATP_synth_b_bact. [Tree]
InterPro	IPR002146. ATPase_F0-cplx_b/b'su_bac. [Graphical view]
KO	K02109.
Pfam	PF00430. ATP-synt_B. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPF_HELPY

Accession

Primary (citable) accession number: P56086

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program