Q03LX7 (ATPF_STRTD) 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:	STER_0517

Organism

Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9) [Complete proteome] [HAMAP]

Taxonomic identifier

322159 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length	165 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 – 165	165	ATP synthase subunit b HAMAP MF_01398		PRO_0000368815
Regions
	Transmembrane	5 – 27	23	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q03LX7 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 2589AEC682E55C36	FASTA	165	18,287
	10 20 30 40 50 60 MSLLINSTTL GNIIITLGSV FLLYYLIRKF AWDQITGIFV AREKKIATDI DSAENARQEA 70 80 90 100 110 120 EILVQKRQEE LAAARTEATQ IIDEAKKTGK TKESKIIAEA YDEAKRLKEK ANQDIAQSWV 130 140 150 160 EALAGVKGEV ADLTVLLAEK VMKQNLDAKA QSDLIDSYLD QLGDA

References

[1]

"Comparative genomics of the lactic acid bacteria." Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V., Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V., Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M., Hawkins T. , Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A., Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W., Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y., Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R., O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T., Richardson P., Kozyavkin S., Weimer B.C., Mills D.A. Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006) [PubMed: 17030793] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-491 / LMD-9.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000419 Genomic DNA. Translation: ABJ65795.1.
RefSeq	YP_819991.1. NC_008532.1.
3D structure databases
ProteinModelPortal	Q03LX7.
ModBase	Search...
Protein-protein interaction databases
STRING	Q03LX7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTRT00000060282; EBSTRP00000055938; EBSTRG00000060272.
GeneID	4437233.
GenomeReviews	Gene locus STER_0517 in contig CP000419_GR.
KEGG	ste:STER_0517.
PATRIC	19798259. VBIStrThe129203_0487.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0711.
GeneTree	EBGT00050000027998.
HOGENOM	HBG617328.
OMA	LEKYNAQ.
ProtClustDB	PRK05759.
Enzyme and pathway databases
BioCyc	STHE322159:STER_0517-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_STRTD

Accession

Primary (citable) accession number: Q03LX7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
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