A1SHI7 (ATPF_NOCSJ) 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:	Noca_1759

Organism

Nocardioides sp. (strain BAA-499 / JS614) [Complete proteome] [HAMAP]

Taxonomic identifier

196162 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Nocardioidaceae › Nocardioides

Protein attributes

Sequence length	189 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 – 189	189	ATP synthase subunit b HAMAP MF_01398		PRO_0000368634
Regions
	Transmembrane	23 – 43	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	A1SHI7 [UniParc]. Last modified February 6, 2007. Version 1. Checksum: 877EB10F6A56A85C	FASTA	189	20,497
	10 20 30 40 50 60 MQALLAAPLA KAEELNPLLP HAIEIVLSLV VFGLLLFAVW KFVTPRFEQI YTERTQAIEG 70 80 90 100 110 120 GLAAAETKQA EADAKLADLE QQLSEARHEA ARIREEAREQ GAQIIAEMRE QAQADAARIV 130 140 150 160 170 180 EHGKTQIEAE RQQAVTSLRA EVGTLATSLA GRIVGESLED DDRSARVVER FLADLETIEA SQAAGGGES

References

[1]

"Complete sequence of chromosome 1 of Nocardioides sp. JS614." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. , Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J., Richardson P. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BAA-499 / JS614.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000509 Genomic DNA. Translation: ABL81272.1.
RefSeq	YP_922959.1. NC_008699.1.
3D structure databases
ProteinModelPortal	A1SHI7.
ModBase	Search...
Protein-protein interaction databases
STRING	A1SHI7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4597941.
GenomeReviews	Gene locus Noca_1759 in contig CP000509_GR.
KEGG	nca:Noca_1759.
PATRIC	22745537. VBINocSp122728_2019.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0711.
HOGENOM	HBG617328.
OMA	LEKYNAQ.
Enzyme and pathway databases
BioCyc	NSP35761:NOCA_1759-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_NOCSJ

Accession

Primary (citable) accession number: A1SHI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 6, 2007
Last modified:	December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program