ID   ATPD_SYNY3              Reviewed;         185 AA.
AC   P27180;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 129.
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};
GN   Synonyms=atpD {ECO:0000255|HAMAP-Rule:MF_01416}; OrderedLocusNames=sll1325;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1832989; DOI=10.1007/bf00037050;
RA   Lill H., Nelson N.;
RT   "The atp1 and atp2 operons of the cyanobacterium Synechocystis sp. PCC
RT   6803.";
RL   Plant Mol. Biol. 17:641-652(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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). CF(0) has four main
CC       subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC       form an alternating ring which encloses part of the gamma chain. F(1)
CC       is 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, b and b'
CC       chains. {ECO:0000255|HAMAP-Rule:MF_01416}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid 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; X58128; CAA41134.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA16736.1; -; Genomic_DNA.
DR   PIR; S17750; PWYBD.
DR   AlphaFoldDB; P27180; -.
DR   SMR; P27180; -.
DR   IntAct; P27180; 1.
DR   STRING; 1148.1651809; -.
DR   PaxDb; P27180; -.
DR   EnsemblBacteria; BAA16736; BAA16736; BAA16736.
DR   KEGG; syn:sll1325; -.
DR   eggNOG; COG0712; Bacteria.
DR   InParanoid; P27180; -.
DR   OMA; MVDNIQD; -.
DR   PhylomeDB; P27180; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0045260; C:plasma membrane proton-transporting ATP synthase complex; IDA:UniProtKB.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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; 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   SUPFAM; SSF47928; SSF47928; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(1); Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Thylakoid; Transport.
FT   CHAIN           1..185
FT                   /note="ATP synthase subunit delta"
FT                   /id="PRO_0000193495"
SQ   SEQUENCE   185 AA;  20093 MW;  F77D9DB601A17F12 CRC64;
     MKGSLYSSKI AEPYAQALIG LAQQQNLTEV FGDNLRSLLT LLQDSPDLSA VLSSPVVKDE
     DKKSVLRSVL GDGGNGYLLN FLMLLVDKRR IVFLEAICEQ YLALLRQFTN TVLAEVTSAL
     KLTDAQKDQV KERVKQLTGA QAVELETKVD GDILGGIVIK VGSQVFDSSL RGQLRRVGLS
     LGTAL