ATPD_KOCRD
ID ATPD_KOCRD Reviewed; 270 AA.
AC B2GLY7;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=ATP synthase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000255|HAMAP-Rule:MF_01416};
GN Name=atpH {ECO:0000255|HAMAP-Rule:MF_01416}; OrderedLocusNames=KRH_09810;
OS Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Kocuria.
OX NCBI_TaxID=378753;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201;
RX PubMed=18408034; DOI=10.1128/jb.01853-07;
RA Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL J. Bacteriol. 190:4139-4146(2008).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC Rule:MF_01416}.
CC -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC It either transmits conformational changes from CF(0) to CF(1) or is
CC implicated in proton conduction. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01416};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01416}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR EMBL; AP009152; BAG29328.1; -; Genomic_DNA.
DR RefSeq; WP_012398049.1; NC_010617.1.
DR AlphaFoldDB; B2GLY7; -.
DR SMR; B2GLY7; -.
DR STRING; 378753.KRH_09810; -.
DR EnsemblBacteria; BAG29328; BAG29328; KRH_09810.
DR KEGG; krh:KRH_09810; -.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_088880_0_0_11; -.
DR OMA; FRFGRIV; -.
DR OrthoDB; 1937493at2; -.
DR Proteomes; UP000008838; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1..270
FT /note="ATP synthase subunit delta"
FT /id="PRO_0000382106"
SQ SEQUENCE 270 AA; 29430 MW; 5BDEBC54543CD301 CRC64;
MAEASNEPYR PLTVDVDRWA AAATPEIAHQ LFEIVDIVDA NGALRRALTD PSRSGEDRAR
LVHTLLDGRA NEVAVDIVAE LASQRSATER QLGDGIERTA VLVAAAAAEN RGGGHALEAL
VDDLIRFKSM LDRSADVQRA FSDSRASAEA KVTLARRLAH TESDEAALLI ERAVSAPRGS
LPGRLLEQFA QWVADRQQRW IARVETARPL GEEQLARLQD GLNRLYGRDL KLTTETNPSL
VGGLRVQVGE EIIDGSLTHR LGQLQQRIGA