A8M2J7 (ATPF_SALAI) 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:	Sare_4016

Organism

Salinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP]

Taxonomic identifier

391037 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micromonosporineae › Micromonosporaceae › Salinispora

Protein attributes

Sequence length	179 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 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 membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete 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 – 179	179	ATP synthase subunit b HAMAP MF_01398		PRO_0000368737
Regions
	Transmembrane	23 – 43	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	A8M2J7 [UniParc]. Last modified December 4, 2007. Version 1. Checksum: 54BE97C74E3D7DC1	FASTA	179	19,483
	10 20 30 40 50 60 MFFLAAEGGE TSHSPILPVW QEIVVGLVAF GLLAFVLMKF VFPRMEQTFQ ARVDAIEGGI 70 80 90 100 110 120 KRAEAAQAEA NQLLEQYRAQ LSEARSDAAK IRDDARADAE GIRQDILAKA REESDRIIAA 130 140 150 160 170 GKEQLVAERA TIVRELRTEV GTLAVDLASK IVGESLADEA RRAGTVDRFL DGLESAGAR

References

[1]

"Complete sequence of Salinispora arenicola CNS-205." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CNS-205.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000850 Genomic DNA. Translation: ABV99806.1.
RefSeq	YP_001538797.1. NC_009953.1.
3D structure databases
ProteinModelPortal	A8M2J7.
ModBase	Search...
Protein-protein interaction databases
STRING	A8M2J7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5707438.
GenomeReviews	Gene locus Sare_4016 in contig CP000850_GR.
KEGG	saq:Sare_4016.
PATRIC	23436603. VBISalAre38676_4053.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG617328.
OMA	LEKYNAQ.
ProtClustDB	CLSK969744.
Enzyme and pathway databases
BioCyc	SARE391037:SARE_4016-MONOMER.
Family and domain databases
HAMAP	MF_01398. ATP_synth_b_bact. [Tree]
InterPro	IPR002146. ATPase_F0-cplx_b/b'su_bac. IPR005864. ATPase_F0-cplx_bsu_bac. [Graphical view]
KO	K02109.
Pfam	PF00430. ATP-synt_B. 1 hit. [Graphical view]
TIGRFAMs	TIGR01144. ATP_synt_b. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ATPF_SALAI

Accession

Primary (citable) accession number: A8M2J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program