ATPD_BACSU
ID ATPD_BACSU Reviewed; 181 AA.
AC P37811;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=BSU36840;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7961438; DOI=10.1128/jb.176.22.6802-6811.1994;
RA Santana M., Ionescu M.S., Vertes A., Longin R., Kunst F., Danchin A.,
RA Glaser P.;
RT "Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and
RT characterization of atp mutants.";
RL J. Bacteriol. 176:6802-6811(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPOIIIJ AND YQJG.
RC STRAIN=168;
RX PubMed=19717609; DOI=10.1128/jb.00853-09;
RA Saller M.J., Fusetti F., Driessen A.J.;
RT "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein
RT biogenesis.";
RL J. Bacteriol. 191:6749-6757(2009).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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 (Probable). The F(1)F(0) complex interacts with SpoIIIJ and YqjG; YqgA
CC is found in the same complex (By similarity) (PubMed:19717609)
CC (Probable). Interacts with FloT (PubMed:23651456). {ECO:0000255|HAMAP-
CC Rule:MF_01416, ECO:0000269|PubMed:19717609,
CC ECO:0000269|PubMed:23651456, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01416,
CC ECO:0000269|PubMed:23651456}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01416}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Peripheral membrane protein.
CC Note=Present in detergent-resistant membrane (DRM) fractions that may
CC be equivalent to eukaryotic membrane rafts; these rafts include
CC proteins involved in signaling, molecule trafficking and protein
CC secretion. {ECO:0000269|PubMed:23651456}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01416}.
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DR EMBL; Z28592; CAA82257.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15701.1; -; Genomic_DNA.
DR PIR; I40365; I40365.
DR RefSeq; NP_391565.1; NC_000964.3.
DR RefSeq; WP_003243176.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P37811; -.
DR SMR; P37811; -.
DR IntAct; P37811; 2.
DR STRING; 224308.BSU36840; -.
DR jPOST; P37811; -.
DR PaxDb; P37811; -.
DR PRIDE; P37811; -.
DR EnsemblBacteria; CAB15701; CAB15701; BSU_36840.
DR GeneID; 936997; -.
DR KEGG; bsu:BSU36840; -.
DR PATRIC; fig|224308.179.peg.3990; -.
DR eggNOG; COG0712; Bacteria.
DR InParanoid; P37811; -.
DR OMA; MVDNIQD; -.
DR PhylomeDB; P37811; -.
DR BioCyc; BSUB:BSU36840-MON; -.
DR SABIO-RK; P37811; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma 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 1: Evidence at protein level;
KW ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1..181
FT /note="ATP synthase subunit delta"
FT /id="PRO_0000193458"
SQ SEQUENCE 181 AA; 19982 MW; 23F8BBAC1E96A7EC CRC64;
MSGSAVSKRY ASALFDIANE SAQLNQVEEE LIVVKQVFQN EKALNDVLNH PKVPAAKKKE
LIQNAFGSLS QSVLNTIFLL IDRHRAAIVP ELTDEFIKLA NVARQTEDAI VYSVKPLTDA
EMLPLSQVFA KKAGVASLRI RNEVQTDLIG GIKVRIGNRI YDGSVSGKLQ RIERQLAGEN
R
