ATP synthase subunit beta - Campylobacter jejuni

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Q0PC30 (ATPB_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. History...

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

Documents (1) |

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:	Cj0107

Organism

Campylobacter jejuni

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	465 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 Reference 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 – 465

465

ATP synthase subunit beta HAMAP MF_01347

PRO_0000339505

Regions

Nucleotide binding

152 – 159

ATP By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q0PC30 [UniParc].

Last modified September 19, 2006. Version 1.
Checksum: 3EC7E58FB7ABE813
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FASTA

465

50,850

        10         20         30         40         50         60 
MQGFISQVLG PVVDVDFNDY LPQINEAIVV NFESEGKKHK LVLEVAAHLG DNRVRTIAMD 

        70         80         90        100        110        120 
MTDGLVRGLK AEALGAPISV PVGEKVLGRI FNVTGDLIDE GEEISFDKKW AIHRDPPAFE 

       130        140        150        160        170        180 
DQSTKSEIFE TGIKVVDLLA PYAKGGKVGL FGGAGVGKTV IIMELIHNVA FKHSGYSVFA 

       190        200        210        220        230        240 
GVGERTREGN DLYNEMKESN VLDKVALCYG QMNEPPGARN RIALTGLTMA EYFRDEMGLD 

       250        260        270        280        290        300 
VLMFIDNIFR FSQSGSEMSA LLGRIPSAVG YQPTLASEMG KFQERITSTK KGSITSVQAV 

       310        320        330        340        350        360 
YVPADDLTDP APATVFAHLD ATTVLNRAIA EKGIYPAVDP LDSTSRMLDP NIIGEEHYKV 

       370        380        390        400        410        420 
ARGVQSVLQK YKDLQDIIAI LGMDELSEED KLVVERARKI EKFLSQPFFV AEVFTGSPGK 

       430        440        450        460 
YISLEDTIAG FKGILEGKYD HLPENAFYMV GNIDEAIAKA DKLKG

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References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M.

Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34278.1.
PIR	C81427.
RefSeq	YP_002343567.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q0PC30.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q0PC30. 17 interactions.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	904437.
GenomeReviews	Gene locus Cj0107 in contig AL111168_GR.
KEGG	cje:Cj0107.
PATRIC	20057141. VBICamJej33762_0105.
Phylogenomic databases
HOGENOM	HBG565875.
OMA	NGNIVQC.
PhylomeDB	Q0PC30.
ProtClustDB	PRK09280.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0107-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_CAMJE

Accession

Primary (citable) accession number: Q0PC30

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	September 19, 2006
Last modified:	January 25, 2012
This is version 48 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

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

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents