ATP6_STRPN
ID ATP6_STRPN Reviewed; 238 AA.
AC P0A2Y8; Q59954; Q933D3; Q93PE9; Q9K3B5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; Synonyms=atpA, uncB;
GN OrderedLocusNames=SP_1513;
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 [GENOMIC DNA].
RC STRAIN=1244, 3180, and 3870;
RX PubMed=10722479; DOI=10.1128/aac.44.4.840-847.2000;
RA Ferrandiz M.J., Fenoll A., Linares J., de la Campa A.G.;
RT "Horizontal transfer of parC and gyrA in fluoroquinolone-resistant clinical
RT isolates of Streptococcus pneumoniae.";
RL Antimicrob. Agents Chemother. 44:840-847(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=310, 606a/R, 606a/S, 654/R, 654/S, 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).
RN [3]
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).
CC -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC in the translocation of protons across the membrane.
CC {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. CF(1) is
CC attached to CF(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_01393}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01393};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01393}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; AF171002; AAF85909.1; -; Genomic_DNA.
DR EMBL; AF171000; AAF85905.1; -; Genomic_DNA.
DR EMBL; AF171001; AAF85907.1; -; Genomic_DNA.
DR EMBL; AF334396; AAK77042.1; -; Genomic_DNA.
DR EMBL; AF334397; AAK77046.1; -; Genomic_DNA.
DR EMBL; AF334391; AAK77032.1; -; Genomic_DNA.
DR EMBL; AF334392; AAK77034.1; -; Genomic_DNA.
DR EMBL; AF334393; AAK77036.1; -; Genomic_DNA.
DR EMBL; AF334394; AAK77038.1; -; Genomic_DNA.
DR EMBL; AF334395; AAK77040.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75604.1; -; Genomic_DNA.
DR PIR; C95176; C95176.
DR RefSeq; WP_000392851.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P0A2Y8; -.
DR SMR; P0A2Y8; -.
DR STRING; 170187.SP_1513; -.
DR EnsemblBacteria; AAK75604; AAK75604; SP_1513.
DR GeneID; 60232645; -.
DR GeneID; 66806603; -.
DR KEGG; spn:SP_1513; -.
DR eggNOG; COG0356; Bacteria.
DR OMA; FTHAVRL; -.
DR PhylomeDB; P0A2Y8; -.
DR BioCyc; SPNE170187:G1FZB-1529-MON; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR045082; ATP_syn_F0_a_bact/chloroplast.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR42823; PTHR42823; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP synthesis; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..238
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082072"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT TRANSMEM 208..230
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT VARIANT 206
FT /note="W -> S (in strain: HV109/R; optochin-resistant)"
SQ SEQUENCE 238 AA; 27208 MW; 15E9AFC691580472 CRC64;
MEESINPIIS IGPVIFNLTM LAMTLLIVGV IFVFIYWASR NMTLKPKGKQ NVLEYVYDFV
IGFTEPNIGS RYMKDYSLFF LCLFLFMVIA NNLGLMTKLQ TIDGTNWWSS PTANLQYDLT
LSFLVILLTH IESVRRRGFK KSIKSFMSPV FVIPMNILEE FTNFLSLALR IFGNIFAGEV
MTSLLLLLSH QAIYWYPVAF GANLAWTAFS VFISCIQAYV FTLLTSVYLG NKINIEEE
