Reviewed, UniProtKB/Swiss-Prot Q92FH0 (ATPA1_LISIN)

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:	lin0136

Organism

Listeria innocua [Complete proteome] [HAMAP]

Taxonomic identifier

1642 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	498 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 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 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 – 498	498	ATP synthase subunit alpha 1 HAMAP MF_01346		PRO_0000238277
Sites
	Site	357	1	Required for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92FH0-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E972B6EA6F6A521D	FASTA	498	54,912
	10 20 30 40 50 60 MKNIHFDINK YEAHVDLEYL KENGRVEKIS DGVIFSSGLE NAALHQAVTI DGRHRGVILE 70 80 90 100 110 120 LNEEFVGIGL IDKTNDILEG MSVSVTDHFI EVNLFEDMAG RIIDTTGKML YDVSDEQPTA 130 140 150 160 170 180 SSPLFCVTPA IMTIDSVTRP LNTGLAVIDS ITPIGRGQRQ LILGNRQSGK TQIAVDTIIN 190 200 210 220 230 240 QHNQNVHCIY VAIGLKAAYI AEVIETLRKH GAMDYSTVVA TAASDSLTAQ YLTPYAGMAV 250 260 270 280 290 300 AEALRDQGKD VLIIFDDLTK HADAYRAITL LFNRPPGREA YPGDSFYIHS SLLERAVQMN 310 320 330 340 350 360 QDHGGGSITA IPMIETLSDD VTAYIPTNVI SITDGQLFLK SDLFNRGQKP AVDVGVSVSR 370 380 390 400 410 420 IGGDAQHPII RKLSKNLTLI LSQYEELKEL LDFGNALDDG SMKMVTDGRM LTELFKQNIL 430 440 450 460 470 480 SPLSVTELIT ILYAFQNGFL TKMAPANVQS FKGLLLEKAH AHQKFEEFSN QIEEISELNE 490 SHVKMLEEII QEAGRPFS

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL596163 Genomic DNA. Translation: CAC95369.1.
PIR	AI1449.
RefSeq	NP_469481.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1128527.
GenomeReviews	Gene locus lin0136 in contig AL592022_GR.
KEGG	lin:lin0136.
NMPDR	fig|272626.1.peg.134.
Organism-specific databases
ListiList	LIN0136.
CMR	Search...
Phylogenomic databases
HOGENOM	Q92FH0.
OMA	DMAGRII.
Enzyme and pathway databases
BioCyc	LINN272626:LIN0136-MON.
BRENDA	3.6.3.14. 270396.
Family and domain databases
HAMAP	MF_01346. [Tree]
InterPro	IPR005294. ATPase_F1-cplx_asu. IPR017458. ATPase_F1-cplx_asu_C. 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. [Graphical view]
TIGRFAMs	TIGR00962. atpA. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPA1_LISIN

Accession

Primary (citable) accession number: Q92FH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 50 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)