HAMAP

Accession	MF_01416
Dates	27-MAR-2009 (Created) 16-AUG-2010 (Last updated, Version 6)

Data class

Protein

Predictors

HAMAP; MF_01416; [distribution of match scores in UniProtKB];[seed alignment for MF_01416]

Names

ATP_synth_delta_bact

Identifier

ATPD

Protein name

RecName: Full=ATP synthase subunit delta; AltName: Full=ATP synthase F(1) sector subunit delta; AltName: Full=F-type ATPase subunit delta; Short=F-ATPase subunit delta;

Protein name

RecName: Full=ATP synthase subunit delta, chloroplastic; AltName: Full=ATP synthase F(1) sector subunit delta; AltName: Full=F-type ATPase subunit delta;

Gene name

atpD

Gene name

atpH, atpD

Gene name

atpH

FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity).

FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction (By similarity).

SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has four main subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta, b and b' chains (By similarity).

SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) 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: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein (By similarity).

SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein (By similarity).

SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein (By similarity).

SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein (By similarity).

SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein (By similarity).

SIMILARITY: Belongs to the ATPase delta chain family.

PROSITE	PS00389; ATPASE_DELTA; 1;
Pfam	PF00213; OSCP; 1;
PRINTS	PR00125; ATPASEDELTA; 1;
TIGRFAMs	TIGR01145; ATP_synt_delta; 1;

ATP synthesis, CF(1), Hydrogen ion transport, Ion transport, Transport.

Thylakoid.

Cell membrane, Cell inner membrane.

Cell membrane.

Cell membrane, Cell inner membrane.

Membrane.

GO:0046933; Molecular function: hydrogen ion transporting ATP synthase activity, rotational mechanism.

GO:0009535; Cellular component: chloroplast thylakoid membrane.

GO:0042651; Cellular component: thylakoid membrane.

GO:0042777; Biological process: plasma membrane ATP synthesis coupled proton transport.
GO:0005886; Cellular component: plasma membrane.

Size range:	157-279 amino acids
Related UniRules:	None
Template:	P0ABA4 (ATPD_ECOLI); P09220 (ATPD_BACP3); P29708 (ATPD_PROMO); P72244 (ATPD_RHOCA); P0A2Z5 (ATPD_STRR6); Q0ZS22 (ATPD_CLOPD): [Recover all]
Scope:	Bacteria Plastid
Fusion:	Nter: MF_01398 (atpF); Cter: None
Duplicate:	in BRAHW, PELCD, PELPD, PHOPR, VIBHB, VIBSL
Plasmid encoded:	None
Comments:	In some of the Mycobacteria one copy is fused with the b subunit. For a review on the peripheral (stator) stalk see PubMed=16730323; DOI=10.1016/j.bbabio.2006.04.007; Weber J.; "ATP synthase: subunit-subunit interactions in the stator stalk."; Biochim. Biophys. Acta 1757:1162-1170(2006).