ATPD1_BRAHW
ID ATPD1_BRAHW Reviewed; 182 AA.
AC C0QW63;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP synthase subunit delta 1 {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta 1 {ECO:0000255|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta 1 {ECO:0000255|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta 1 {ECO:0000255|HAMAP-Rule:MF_01416};
GN Name=atpH1 {ECO:0000255|HAMAP-Rule:MF_01416};
GN OrderedLocusNames=BHWA1_02191;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(2009).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; CP001357; ACN84649.1; -; Genomic_DNA.
DR RefSeq; WP_012671681.1; NC_012225.1.
DR AlphaFoldDB; C0QW63; -.
DR SMR; C0QW63; -.
DR STRING; 565034.BHWA1_02191; -.
DR EnsemblBacteria; ACN84649; ACN84649; BHWA1_02191.
DR GeneID; 63963346; -.
DR KEGG; bhy:BHWA1_02191; -.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_085114_3_0_12; -.
DR OMA; MINAQAF; -.
DR Proteomes; UP000001803; 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 Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Transport.
FT CHAIN 1..182
FT /note="ATP synthase subunit delta 1"
FT /id="PRO_0000382065"
SQ SEQUENCE 182 AA; 20871 MW; C9D6AA3D818147C1 CRC64;
MKESDKLQIL KPTASAIFDI ARELGMIKEI YNELSECSKL FQDIDIKKYF FDKSISKKDK
KELIDKRLKP ILSKETYAFV SILTEHDSID VLPDIVALYK EIADDYSNIV RVRIITASTI
DDKTVEDIIQ TVKCFSSNEI SYETIVDENI IGGIIVYIGS VVYDYSIKKQ IDLLQSKFTY
GN