Q92G88 (ATPB_RICCN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit beta
EC=3.6.3.14

Alternative name(s):
ATP synthase F1 sector subunit beta
F-ATPase subunit beta

Gene names

Name:	atpD
Ordered Locus Names:	RC1235

Organism

Rickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]

Taxonomic identifier

272944 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group › Rickettsia conorii

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits By similarity. HAMAP-Rule MF_01347
Catalytic activity	ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01347
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 HAMAP-Rule MF_01347.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.
Sequence caution	The sequence AAL03773.1 differs from that shown. Reason: Erroneous initiation.

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	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro plasma membrane ATP synthesis coupled proton transport Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell 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 proton-transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 473	473	ATP synthase subunit beta HAMAP-Rule MF_01347		PRO_0000144465
Regions
	Nucleotide binding	153 – 160	8	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q92G88 [UniParc]. Last modified February 11, 2002. Version 2. Checksum: 416BAF37EE497CB2	FASTA	473	51,108
	10 20 30 40 50 60 MTKNIGKITQ IISAVVDVKF TNNGELPKIL NALECYNDKQ RIVLEVAQHI GDDTVRCIAM 70 80 90 100 110 120 DSMEGLVRGV EVIDTGSPIR IPVGTETLGR IMNVVGEPID GKGDIKSSNI SSIYKPAPDF 130 140 150 160 170 180 THQSTECNIL VTGIKVIDLL APYTKGGKIG LFGGAGVGKT VLIMELINNV AKAHGGYTVF 190 200 210 220 230 240 AGVGERTREG NDLYHEMIDS GVINLAEPEK SKVALVYGQM NEPPGARARV ALSGLTIAES 250 260 270 280 290 300 FRDMNEGQDV LFFVDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGE LQERITSTKY 310 320 330 340 350 360 GSITSVQAIY VPADDLTDPA PATSFAHLDA TTVLSRQIAE FGIYPAVDPL DSNSQVLDPM 370 380 390 400 410 420 IVGEEHYSVA RQVQQVLQTY KSLQDIITIL GMDELSEEDK LTVARARKIQ RFLSQPFHVA 430 440 450 460 470 EVFTGAAGKF VNLADTIAGF KGLVEGKYDD LPEAAFYMVG TIDEAIEKAQ TLK

References

[1]

"Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE006914 Genomic DNA. Translation: AAL03773.1. Different initiation.
PIR	C97854.
RefSeq	NP_360872.1. NC_003103.1.
3D structure databases
ProteinModelPortal	Q92G88.
SMR	Q92G88. Positions 6-463.
ModBase	Search...
Protein-protein interaction databases
STRING	272944.RC1235.
Proteomic databases
PRIDE	Q92G88.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL03773; AAL03773; RC1235.
GeneID	928389.
KEGG	rco:RC1235.
PATRIC	17889970. VBIRicCon45613_1416.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0055.
HOGENOM	HOG000009605.
KO	K02112.
OMA	NNIAKGH.
ProtClustDB	PRK09280.
Family and domain databases
Gene3D	1.10.1140.10. 1 hit.
HAMAP	MF_01347. ATP_synth_beta_bact.
InterPro	IPR003593. AAA+_ATPase. IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR005722. ATPase_F1-cplx_bsu. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
PANTHER	PTHR15184:SF8. PTHR15184:SF8. 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]
SMART	SM00382. AAA. 1 hit. [Graphical view]
SUPFAM	SSF47917. ATPase_a/b_C. 1 hit. SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMs	TIGR01039. atpD. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPB_RICCN

Accession

Primary (citable) accession number: Q92G88

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 11, 2002
Last sequence update:	February 11, 2002
Last modified:	May 1, 2013
This is version 84 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program