Q79VG9 (ATPF_CORGL) 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:	Cgl1208, cg1364

Organism

Corynebacterium glutamicum (Brevibacterium flavum)

Taxonomic identifier

1718 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length	188 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 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 – 188	188	ATP synthase subunit b HAMAP MF_01398		PRO_0000368438
Regions
	Transmembrane	30 – 50	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q79VG9 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 929763AD77D486E0	FASTA	188	21,095
	10 20 30 40 50 60 MANSIYNLAQ ADALPLESGN SILFPPLYDI VWSLIPFLII LIVFWKLVLP KFQEVLTERE 70 80 90 100 110 120 DRIKGGIQRA EAAQAEAKAA LEKYNAQLAE ARTEAAEIRE QARERGKQIE AELKDKANEE 130 140 150 160 170 180 SNRIIESGSK QLLAQREQVV NELRREMGQN SINLAEHLLG DQLSDNVKRS GTIDRFLADL DTVAPNGK

References

[1]

"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

[2]

"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A. J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB046112 Genomic DNA. Translation: BAB08153.1. BA000036 Genomic DNA. Translation: BAB98601.1. BX927151 Genomic DNA. Translation: CAF19912.1.
RefSeq	NP_600433.1. NC_003450.3. YP_225498.1. NC_006958.1.
3D structure databases
ProteinModelPortal	Q79VG9.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1019191. 3343872.
GenomeReviews	Gene locus Cgl1208 in contig BA000036_GR. Gene locus cg1364 in contig BX927147_GR.
KEGG	cgb:cg1364. cgl:NCgl1161.
PATRIC	21494462. VBICorGlu203724_1187.
Phylogenomic databases
HOGENOM	HBG617328.
OMA	LEKYNAQ.
ProtClustDB	PRK05759.
Enzyme and pathway databases
BioCyc	CGLU196627:CG1364-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_CORGL

Accession

Primary (citable) accession number: Q79VG9
Secondary accession number(s): Q9FDR8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program