ID D6YWH1_WADCW Unreviewed; 182 AA.
AC D6YWH1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=ATP synthase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
GN Name=atpH {ECO:0000256|HAMAP-Rule:MF_01416,
GN ECO:0000313|EMBL:ADI38482.1};
GN OrderedLocusNames=wcw_1125 {ECO:0000313|EMBL:ADI38482.1};
OS Waddlia chondrophila (strain ATCC VR-1470 / WSU 86-1044).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Waddliaceae; Waddlia.
OX NCBI_TaxID=716544 {ECO:0000313|EMBL:ADI38482.1, ECO:0000313|Proteomes:UP000001505};
RN [1] {ECO:0000313|EMBL:ADI38482.1, ECO:0000313|Proteomes:UP000001505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1470 / WSU 86-1044 {ECO:0000313|Proteomes:UP000001505};
RX PubMed=20531937; DOI=10.1371/journal.pone.0010890;
RA Bertelli C., Collyn F., Croxatto A., Ruckert C., Polkinghorne A.,
RA Kebbi-Beghdadi C., Goesmann A., Vaughan L., Greub G.;
RT "The Waddlia genome: a window into chlamydial biology.";
RL PLoS ONE 5:E10890-E10890(2010).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01416}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01416}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01416}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01416}.
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DR EMBL; CP001928; ADI38482.1; -; Genomic_DNA.
DR RefSeq; WP_013182195.1; NZ_LVEB01000021.1.
DR AlphaFoldDB; D6YWH1; -.
DR STRING; 716544.wcw_1125; -.
DR KEGG; wch:wcw_1125; -.
DR eggNOG; COG0712; Bacteria.
DR HOGENOM; CLU_085114_1_1_0; -.
DR Proteomes; UP000001505; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 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 NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
PE 3: Inferred from homology;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW Rule:MF_01416}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01416};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW Rule:MF_01416}; Hydrolase {ECO:0000313|EMBL:ADI38482.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_01416};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01416};
KW Reference proteome {ECO:0000313|Proteomes:UP000001505};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ SEQUENCE 182 AA; 21074 MW; EB3B70849B0EC769 CRC64;
MTKASTKYAG ILFFLALKKQ ELETYLFQLQ EIKKITSNTH LQEAFASPLV PLQAKKNVLE
LLFKDKVKEE ILLFLKILTE QKKISLITEV IEEFSIKMKK QMGILSIKLI SAEKIDEENK
LLLQNKLEAK YNKKIEFYEE QSSKIIGGMI LLFPNGKILD KSLKTCLEHL RKHLKKGKRH
AA
//
