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ATPA_CORA7
ID   ATPA_CORA7              Reviewed;         546 AA.
AC   C3PFR3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=cauri_1072;
OS   Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS   CN-1) (Corynebacterium nigricans).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=548476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1;
RX   PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA   Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA   Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA   Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT   "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT   aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT   vaginal swab of a woman with spontaneous abortion.";
RL   BMC Genomics 11:91-91(2010).
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; CP001601; ACP32667.1; -; Genomic_DNA.
DR   RefSeq; WP_010187069.1; NZ_ACLH01000006.1.
DR   AlphaFoldDB; C3PFR3; -.
DR   SMR; C3PFR3; -.
DR   STRING; 548476.cauri_1072; -.
DR   PRIDE; C3PFR3; -.
DR   EnsemblBacteria; ACP32667; ACP32667; cauri_1072.
DR   GeneID; 31923694; -.
DR   KEGG; car:cauri_1072; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_11; -.
DR   OMA; LQAPGVM; -.
DR   OrthoDB; 837522at2; -.
DR   Proteomes; UP000002077; 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: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; IPR020003; ATPase_a/bsu_AS.
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   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; Cell membrane; CF(1); Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Reference proteome;
KW   Translocase; Transport.
FT   CHAIN           1..546
FT                   /note="ATP synthase subunit alpha"
FT                   /id="PRO_1000166532"
FT   REGION          511..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         172..179
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            373
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   546 AA;  58670 MW;  F9A3BA7700BB3A80 CRC64;
     MAELTISSDE IRSAIANYTS SYSAEASREE VGVVISAADG IAQVSGLPSV MANELLEFPG
     GVIGVAQNLD TNSIGVVVLG NFESLKEGDE VKRTGEVLSI PVGEEFLGRV INPLGQPIDG
     MGPITAEEDR VLELQAPSVL QRQPVEEPMQ TGIKAIDAMT PIGRGQRQLI IGDRKTGKTA
     VCIDTILNQK ANWESGDKNK QVRCIYVAIG QKGSTIAGVR HTLEQHGALE YTTIVAAPAS
     DAAGFKWLAP FSGAALGQHW MYQGNHVLII YDDLTKQAEA YRAISLLLRR PPGREAYPGD
     VFYLHSRLLE RAAKLSDDMG AGSMTALPII ETKANDVSAF IPTNVISITD GQVFLESDLF
     NQGVRPAINV GVSVSRVGGA AQTKGMKKVA GNLRLELAAY RDLQAFAAFA SDLDPASKAQ
     LERGERLVEL LKQSESSPQP VEYQMVSIFL ADQGIFDVVP VEDVRRFEKE LHDHLNSATP
     QVFEQIQGGT ALTDESKDAL VAAAKDFTPS FRTTEGNNLG TEAPVDPLAA DDVNKTELNV
     SRKTAK
 
 
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