ATPD_STRPN
ID ATPD_STRPN Reviewed; 178 AA.
AC P0A2Z4; Q54785;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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}; Synonyms=atpX;
GN OrderedLocusNames=SP_1511;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-91.
RC STRAIN=M222;
RX PubMed=7934882; DOI=10.1111/j.1365-2958.1994.tb01045.x;
RA Fenoll A., Munoz R., Garcia E., de la Campa A.G.;
RT "Molecular basis of the optochin-sensitive phenotype of pneumococcus:
RT characterization of the genes encoding the F0 complex of the Streptococcus
RT pneumoniae and Streptococcus oralis H(+)-ATPases.";
RL Mol. Microbiol. 12:587-598(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RC STRAIN=HV109/R, and HV109/S;
RX PubMed=11474432; DOI=10.1086/322803;
RA Pikis A., Campos J.M., Rodriguez W.J., Keith J.M.;
RT "Optochin resistance in Streptococcus pneumoniae: mechanism, significance,
RT and clinical implications.";
RL J. Infect. Dis. 184:582-590(2001).
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; AE005672; AAK75602.1; -; Genomic_DNA.
DR EMBL; Z26850; CAA81450.1; -; Genomic_DNA.
DR EMBL; AF334396; AAK77044.1; -; Genomic_DNA.
DR EMBL; AF334397; AAK77048.1; -; Genomic_DNA.
DR PIR; A95176; A95176.
DR PIR; S49402; S49402.
DR RefSeq; WP_000359036.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A2Z4; -.
DR SMR; P0A2Z4; -.
DR STRING; 170187.SP_1511; -.
DR DNASU; 931327; -.
DR EnsemblBacteria; AAK75602; AAK75602; SP_1511.
DR GeneID; 60233318; -.
DR GeneID; 66806601; -.
DR KEGG; spn:SP_1511; -.
DR eggNOG; COG0712; Bacteria.
DR OMA; QVIVAHE; -.
DR PhylomeDB; P0A2Z4; -.
DR BioCyc; SPNE170187:G1FZB-1527-MON; -.
DR Proteomes; UP000000585; 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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Transport.
FT CHAIN 1..178
FT /note="ATP synthase subunit delta"
FT /id="PRO_0000193491"
FT CONFLICT 6
FT /note="V -> A (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="L -> I (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="T -> D (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="V -> A (in Ref. 2; CAA81450 and 3; AAK77044/
FT AAK77048)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="K -> E (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="K -> A (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 63..64
FT /note="IA -> VG (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="L -> M (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="A -> I (in Ref. 2; CAA81450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 178 AA; 20541 MW; CB048FAF2E4E42B1 CRC64;
MDKKTVKVIE KYSMPFVQLV LEKGEEDRIF SDLTQIKQVV EKTGLPSFLK QVAVDESDKE
KTIAFFQDSV SPLLQNFIQV LAYNHRANLF YDVLVDCLNR LEKETNRFEV TITSAHPLTD
EQKTRLLPLI EKKMSLKVRS VKEQIDESLI GGFVIFANHK TIDVSIKQQL KVVKENLK
