ATP synthase subunit beta - Rickettsia bellii (strain RML369-C)

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Q1RKD7 (ATPB_RICBR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	RBE_0096

Organism

Rickettsia bellii (strain RML369-C) [Complete proteome] [HAMAP]

Taxonomic identifier

336407 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia

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 MF_01347
Catalytic activity	ATP + H₂O + H⁺(In) = ADP + phosphate + H⁺(Out). HAMAP 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 MF_01347.
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	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
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: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from electronic annotation. Source: InterPro 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 – 473

473

ATP synthase subunit beta HAMAP MF_01347

PRO_0000254362

Regions

Nucleotide binding

153 – 160

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q1RKD7 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 7D613C04E182B855
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FASTA

473

51,113

        10         20         30         40         50         60 
MKKNIGKITQ IISAVVDVKF TNKGKLPQIL NALECYNDKQ RIVLEIAQHI GDDTVRCIAM 

        70         80         90        100        110        120 
NSTEGLVRGM EVVDTGSPIS IPVGIETLGR IMNVVGEPID GKGKIKGSSI SSIYKSAPSF 

       130        140        150        160        170        180 
TQQSTDRNIL VTGIKVVDLL APYTKGGKIG LFGGAGVGKT VLIMELINNV AKAHGGYTVF 

       190        200        210        220        230        240 
AGVGERTREG NDLYHEMIDS GVINLEEPEK SKVALVYGQM NEPPGARARV ALTGLTVAES 

       250        260        270        280        290        300 
FRDMNEGQDV LFFVDNIFRF TQAGSEVSAL LGRIPSAVGY QPTLATDMGE LQERITSTKH 

       310        320        330        340        350        360 
GSITSVQAIY VPADDLTDPA PATSFAHLDA TTVLSRQIAE LGIYPAVDPL DSTSQVLDPM 

       370        380        390        400        410        420 
IVGEEHYNVA RKVQQILQTY KSLQDIIAIL GMDELSEEDK LTVSRARKIQ RFLSQPFHVA 

       430        440        450        460        470 
EVFTGAEGKF VNLADTIAGF KGLTEGKYDD LPEAAFYMVG TIEEALEKAK TLK

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References

[1]

"Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
PLoS Genet. 2:733-744(2006) [PubMed: 16703114] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RML369-C.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000087 Genomic DNA. Translation: ABE04177.1.
RefSeq	YP_537266.1. NC_007940.1.
3D structure databases
HSSP	HSSP built from PDB template 2F43 based on UniProtKB P10719.
ProteinModelPortal	Q1RKD7.
SMR	Q1RKD7. Positions 6-463.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1RKD7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3995630.
GenomeReviews	Gene locus RBE_0096 in contig CP000087_GR.
KEGG	rbe:RBE_0096.
PATRIC	17881448. VBIRicBel102610_0108.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0055.
HOGENOM	HBG565875.
OMA	QVLDPMI.
ProtClustDB	PRK09280.
Enzyme and pathway databases
BioCyc	RBEL336407:RBE_0096-MONOMER.
Family and domain databases
HAMAP	MF_01347. ATP_synth_beta_bact. [Tree]
InterPro	IPR020003. ATPase_a/bsu_AS. IPR003593. ATPase_AAA+_core. IPR005722. ATPase_F1-cplx_bsu. IPR018118. ATPase_F1/A1-cplx_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR024034. ATPase_F1_bsu/V1_C. [Graphical view]
Gene3D	G3DSA:1.10.1140.10. G3DSA:1.10.1140.10. 1 hit.
KO	K02112.
PANTHER	PTHR15184:SF8. ATPase_F1_b. 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_RICBR

Accession

Primary (citable) accession number: Q1RKD7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	May 16, 2006
Last modified:	January 25, 2012
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Rickettsia bellii strain RML369-C

Rickettsia bellii (strain RML369-C): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents