ATPA_STRA1
ID ATPA_STRA1 Reviewed; 501 AA.
AC Q3K1J7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=ATP synthase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346}; OrderedLocusNames=SAK_0984;
OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS SS700).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=205921;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27591 / A909 / CDC SS700;
RX PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA Wessels M.R., Rappuoli R., Fraser C.M.;
RT "Genome analysis of multiple pathogenic isolates of Streptococcus
RT agalactiae: implications for the microbial 'pan-genome'.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(2005).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The alpha chain is a regulatory subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
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_01346}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01346};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; CP000114; ABA44763.1; -; Genomic_DNA.
DR RefSeq; WP_000996613.1; NC_007432.1.
DR AlphaFoldDB; Q3K1J7; -.
DR SMR; Q3K1J7; -.
DR GeneID; 66885811; -.
DR KEGG; sak:SAK_0984; -.
DR HOGENOM; CLU_010091_2_1_9; -.
DR OMA; LQAPGVM; -.
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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd01132; F1_ATPase_alpha; 1.
DR Gene3D; 1.20.150.20; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR033732; ATP_synth_F1_a.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF00306; ATP-synt_ab_C; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00962; atpA; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..501
FT /note="ATP synthase subunit alpha"
FT /id="PRO_0000238361"
FT BINDING 169..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 362
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 501 AA; 54607 MW; CCDB4D46118B0082 CRC64;
MAINAQEISA LIKKQIEDFQ PNFDVTETGI VTYIGDGIAR ARGLDNAMSG ELLEFSNGAY
GMAQNLESND VGIIILGDFS EIREGDVVKR TGKIMEVPVG EAMIGRVVNP LGQPVDGLGE
IETTATRPVE TPAPGVMQRK SVFEPLQTGL KAIDALVPIG RGQRELIIGD RQTGKTSVAI
DAILNQKGQD MICIYVAIGQ KESTVRTQVE TLRKYGALDY TIVVTASASQ PSPLLFIAPY
AGVAMAEEFM YNGKHVLIVY DDLSKQAVAY RELSLLLRRP PGREAYPGDV FYLHSRLLER
SAKVSDALGG GSITALPFIE TQAGDISAYI ATNVISITDG QIFLQENLFN SGIRPAIDAG
SSVSRVGGAA QIKAMKRVAG TLRLDLASYR ELEAFTQFGS DLDAATQAKL NRGRRTVEVL
KQPLHKPLPV EKQVVILYAL THGFLDDVPV NDILAFEEAL YDYFDAHYDN LFETIRTTKD
LPEEAELDAA IQAFKDQSQF K
