ATP6_STRR6
ID ATP6_STRR6 Reviewed; 238 AA.
AC P0A2Y9; 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 101.
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=spr1365;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [2]
RP SEQUENCE REVISION TO 104.
RA Garcia E.;
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=11580837; DOI=10.1046/j.1365-2958.2001.02597.x;
RA Martin-Galiano A.J., Ferrandiz M.J., de la Campa A.G.;
RT "The promoter of the operon encoding the F0F1 ATPase of Streptococcus
RT pneumoniae is inducible by pH.";
RL Mol. Microbiol. 41:1327-1338(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(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, ECO:0000269|PubMed:11580837}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11580837};
CC Multi-pass membrane protein {ECO:0000305|PubMed:11580837}.
CC -!- INDUCTION: Induced by a decrease in external pH from 7.5 to 5.7.
CC {ECO:0000269|PubMed:11580837}.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01393}.
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DR EMBL; Z26851; CAA81453.2; -; Genomic_DNA.
DR EMBL; AF334388; AAK77028.1; -; Genomic_DNA.
DR EMBL; AF368465; AAL66412.1; -; Genomic_DNA.
DR EMBL; AE007317; AAL00169.1; -; Genomic_DNA.
DR PIR; D98042; D98042.
DR PIR; S49405; S49405.
DR RefSeq; NP_358958.1; NC_003098.1.
DR RefSeq; WP_000392851.1; NC_003098.1.
DR AlphaFoldDB; P0A2Y9; -.
DR SMR; P0A2Y9; -.
DR STRING; 171101.spr1365; -.
DR EnsemblBacteria; AAL00169; AAL00169; spr1365.
DR GeneID; 60232645; -.
DR GeneID; 66806603; -.
DR KEGG; spr:spr1365; -.
DR PATRIC; fig|171101.6.peg.1479; -.
DR eggNOG; COG0356; Bacteria.
DR HOGENOM; CLU_041018_2_3_9; -.
DR OMA; FTHAVRL; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW Antibiotic resistance; ATP synthesis; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..238
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082073"
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 CONFLICT 104
FT /note="G -> E (in Ref. 4; AAL66412)"
FT /evidence="ECO:0000305"
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
