Reviewed, UniProtKB/Swiss-Prot Q5FRC7 (ATPA1_GLUOX)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit alpha 1
    EC=3.6.3.14
Alternative name(s):
    F-ATPase subunit alpha 1
    ATP synthase F1 sector subunit alpha 1

Gene names

Name:	atpA1
Ordered Locus Names:	GOX1311

Organism

Gluconobacter oxydans (Gluconobacter suboxydans) [Complete proteome] [HAMAP]

Taxonomic identifier

442 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit By similarity.
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01346
Subunit structure	F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a1, b2 and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF1 is attached to CF0 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; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW proton-transporting ATP synthase complex, catalytic core F(1) Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP proton-transporting ATPase activity, rotational mechanism 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 – 511	511	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000238258
Regions
	Nucleotide binding	170 – 177	8	ATP By similarity
Sites
	Site	371	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5FRC7-1 [UniParc]. Last modified March 1, 2005. Version 1. Checksum: ACBC5BEE20FD3F8F	FASTA	511	54,952
	10 20 30 40 50 60 MDIRPAEISD ILKQQIASFD QVETVSETGT VLSIGDGIAR VYGLTNVMAG EMVEFEGTGL 70 80 90 100 110 120 KGMALNLEAD NVGVVLFGDG DSIREGDTVL RTKSVVEVPV GKGLLGRVVD GLGNPIDGRG 130 140 150 160 170 180 PLTDVEYRRA EVKAPGIMPR QSVSEPMQTG IKAIDALVPI GRGQRELIIG DRQTGKTAIL 190 200 210 220 230 240 IDTIVAQKPV NAEGDPKKSL YCIYVAVGQK RSTVANLVRT LIEHGAMEYS IVVAATASDA 250 260 270 280 290 300 APMQYLAPYT ACAMGEYFRD NGMHALVCYD DLSKQAVAYR QMSLLLRRPP AREAFPGDVF 310 320 330 340 350 360 YLHSRLLERA AKMSDANGGG SLTALPVIET QAGDTAAYIP TNVISITDGQ IFLETDLFYR 370 380 390 400 410 420 GIRPAVNVGG SVSRVGSAAQ IKAMKQVAGK IKLELAQYRE MAAFSQFASD LDAATRKQLD 430 440 450 460 470 480 RGARLVELLK QPETSPLPVE EQVVVLYAGT RGYVDPIAVD KVVAYEAALL SELRGAGSDI 490 500 510 LTAIRNDRQI KPETEGKLKE LLEAFGKRFS A

References

[1]

"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans." Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U. Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 621H.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000009 Genomic DNA. Translation: AAW61069.1.
RefSeq	YP_191725.1.
3D structure databases
SMR	Q5FRC7. Positions 25-511.
ModBase	Search...
Genome annotation databases
GeneID	3250774.
GenomeReviews	Gene locus GOX1311 in contig CP000009_GR.
KEGG	gox:GOX1311.
NMPDR	fig|290633.1.peg.1270.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5FRC7.
OMA	KQVAIIF.
Enzyme and pathway databases
BioCyc	GOXY290633:GOX1311-MON.
BRENDA	3.6.3.14. 3050.
Family and domain databases
HAMAP	MF_01346. [Tree]
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR020003. ATPase_F1/V1/A1_a/bsu_AS. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. [Graphical view]
PANTHER	PTHR15184:SF3. ATPase_F1_a. 1 hit.
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA1_GLUOX

Accession

Primary (citable) accession number: Q5FRC7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	March 1, 2005
Last modified:	November 3, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)