ATP synthase subunit beta - Helicobacter pylori (strain ATCC 700392 / 26695)

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P55988 (ATPB_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. 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:	HP_1132

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length	469 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 – 469

469

ATP synthase subunit beta HAMAP MF_01347

PRO_0000144444

Regions

Nucleotide binding

155 – 162

ATP By similarity

Natural variations

Natural variant

73 – 74

VI → AV in strain: CCUG 17874 / NCTC 11638.

Natural variant

363

V → I in strain: CCUG 17874 / NCTC 11638.

Sequences

Sequence

Length

Mass (Da)

Tools

P55988 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: CEF654B885738181
Show »

FASTA

469

51,478

        10         20         30         40         50         60 
MKAMEGKIIQ VLGPVVDVEF ESYLPAIFEA LDINFEVNGV QKSLVLEVAA HLGGNRVRAI 

        70         80         90        100        110        120 
AMDMTEGLVR NQVIKARGKM IEVPVGEEVL GRIFNVVGES IDNLEPLKPS LTWPIHRKAP 

       130        140        150        160        170        180 
SFEQQSTKTE MFETGIKVID LLAPYSKGGK VGLFGGAGVG KTVIIMELIH NVAYKHNGYS 

       190        200        210        220        230        240 
VFAGVGERTR EGNDLYFEMK EGGVLDKVAL CYGQMNEPPG ARNRIAFTGL TMAEYFRDEK 

       250        260        270        280        290        300 
GLDVLMFIDN IFRYAQSGAE MSALLGRIPS AVGYQPTLAG EMGKLQERIA STKNGSITSV 

       310        320        330        340        350        360 
QAVYVPADDL TDPAPASVFA HLDATTVLNR KIAEKGIYPA VDPLDSTSRI LSPQMIGEKH 

       370        380        390        400        410        420 
YEVATGIQQV LQKYKDLQDI IAILGLDELS EEDKKTVERA RKIEKFLSQP FFVAEVFTGS 

       430        440        450        460 
PGKYVTLQET LEGFGGILEG KYDHIPENAF YMVGSIQEVL EKAKNMKNS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of F1F0-ATPase from Helicobacter pylori." McGowan C.C., Cover T.L., Blaser M.J. Infect. Immun. 65:2640-2647(1997) [PubMed: 9199431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 4867 / CCUG 17874 / NCTC 11638.
[2]	"The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C. Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF004014 Genomic DNA. Translation: AAB61298.1. AE000511 Genomic DNA. Translation: AAD08174.1.
PIR	D64661.
RefSeq	NP_207923.1. NC_000915.1.
3D structure databases
ProteinModelPortal	P55988.
SMR	P55988. Positions 5-466.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3361N.
MINT	MINT-162973.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	899669.
GenomeReviews	Gene locus HP_1132 in contig AE000511_GR.
KEGG	hpy:HP1132.
NMPDR	fig\|85962.1.peg.1119.
PATRIC	20593609. VBIHelPyl33062_1184.
TIGR	HP_1132.
Phylogenomic databases
HOGENOM	HBG565875.
OMA	IGQEHYD.
ProtClustDB	PRK09280.
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_HELPY

Accession

Primary (citable) accession number: P55988
Secondary accession number(s): O07676

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 92 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

Helicobacter pylori

Helicobacter pylori (strain 26695): 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

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents