Reviewed, UniProtKB/Swiss-Prot Q8YJ38 (ATPD_BRUME)

Names and origin

Protein names

Recommended name:
    ATP synthase subunit delta
Alternative name(s):
    ATP synthase F(1) sector subunit delta
    F-type ATPase subunit delta
      Short name=F-ATPase subunit delta

Gene names

Name:	atpH
Ordered Locus Names:	BMEI0248

Organism

Brucella melitensis [Complete proteome] [HAMAP]

Taxonomic identifier

29459 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length	186 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	F1F0 ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F1 containing the extramembraneous catalytic core and F0 containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation By similarity. This protein is part of the stalk that links CF0 to CF1. It either transmits conformational changes from CF0 to CF1 or is implicated in proton conduction By similarity.
Subunit structure	F-type ATPases have 2 components, F1 - the catalytic core - and F0 - the membrane proton channel. F1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. F0 has three main subunits: a1, b2 and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F1 is attached to F0 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.
Sequence similarities	Belongs to the ATPase delta chain family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Cell inner membrane Cell membrane Membrane
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro
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	hydrogen ion 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 – 186	186	ATP synthase subunit delta HAMAP MF_01416		PRO_1000184661

Sequences

	Sequence		Length	Mass (Da)
	Q8YJ38-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 225806A68B4245EA	FASTA	186	19,564
	10 20 30 40 50 60 MAETSSLISG VAQRCAGSLF ELALDANSVA SVEKDLGRFE ALLSGSEDLR RLISSPVFSS 70 80 90 100 110 120 EDQLHAIGAI ADKAGIKGLV GNFLRVVAQN RRLFALPGII AAFRQIAAEH RGEISADVVS 130 140 150 160 170 180 AHELTSAQQN ELKATLKGVA GKDVTINVTV DPSILGGLIV KMGSRQIDTS LRTKLSSLKL ALKEVG

References

[1]

"The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. , Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J., Haselkorn R., Kyrpides N.C., Overbeek R. Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094 / Biotype 1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE008917 Genomic DNA. Translation: AAL51430.1.
PIR	AC3283.
RefSeq	NP_539166.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1195960.
GenomeReviews	Gene locus BMEI0248 in contig AE008917_GR.
KEGG	bme:BMEI0248.
NMPDR	fig|224914.1.peg.248.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG668108.
OMA	GELFVQV.
PhylomeDB	Q8YJ38.
Enzyme and pathway databases
BioCyc	BMEL224914:BMEI0248-MON.
Family and domain databases
HAMAP	MF_01416. [Tree]
InterPro	IPR000711. ATPase_F1-cplx_OSCP/dsu. IPR020781. ATPase_F1-cplx_OSCP/dsu_CS. [Graphical view]
Gene3D	G3DSA:1.10.520.20. ATPase_F1_OSCP/d. 1 hit.
PANTHER	PTHR11910. ATPase_F1_OSCP/d. 1 hit.
Pfam	PF00213. OSCP. 1 hit. [Graphical view]
PRINTS	PR00125. ATPASEDELTA.
PROSITE	PS00389. ATPASE_DELTA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATPD_BRUME

Accession

Primary (citable) accession number: Q8YJ38

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	March 1, 2002
Last modified:	December 15, 2009
This is version 48 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)