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Database: UniProt
Entry: X5EB05_9CORY
LinkDB: X5EB05_9CORY
Original site: X5EB05_9CORY 
ID   X5EB05_9CORY            Unreviewed;       544 AA.
AC   X5EB05;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=ATP synthase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346,
GN   ECO:0000313|EMBL:AHW63791.1};
GN   ORFNames=CGLY_06730 {ECO:0000313|EMBL:AHW63791.1};
OS   Corynebacterium glyciniphilum AJ 3170.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1404245 {ECO:0000313|EMBL:AHW63791.1, ECO:0000313|Proteomes:UP000023703};
RN   [1] {ECO:0000313|EMBL:AHW63791.1, ECO:0000313|Proteomes:UP000023703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AJ 3170 {ECO:0000313|EMBL:AHW63791.1};
RX   PubMed=25323597; DOI=10.1099/ijs.0.065102-0;
RA   Al-Dilaimi A., Bednarz H., Lomker A., Niehaus K., Kalinowski J.,
RA   Ruckert C.;
RT   "Revisiting Corynebacterium glyciniphilum (ex Kubota et al., 1972) sp.
RT   nov., nom. rev., isolated from putrefied banana.";
RL   Int. J. Syst. Evol. Microbiol. 65:177-182(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_01346};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01346};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346}.
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DR   EMBL; CP006842; AHW63791.1; -; Genomic_DNA.
DR   RefSeq; WP_038551785.1; NZ_CP006842.1.
DR   AlphaFoldDB; X5EB05; -.
DR   STRING; 1404245.CGLY_06730; -.
DR   KEGG; cgy:CGLY_06730; -.
DR   eggNOG; COG0056; Bacteria.
DR   HOGENOM; CLU_010091_2_1_11; -.
DR   OrthoDB; 9803053at2; -.
DR   Proteomes; UP000023703; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; cd18116; ATP-synt_F1_alpha_N; 1.
DR   CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_nt-bd_dom.
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   NCBIfam; TIGR00962; atpA; 1.
DR   PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01346};
KW   Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346};
KW   Hydrolase {ECO:0000313|EMBL:AHW63791.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01346};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01346}; Reference proteome {ECO:0000313|Proteomes:UP000023703};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_01346};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01346}.
FT   DOMAIN          29..95
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          152..375
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          382..507
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
FT   REGION          511..544
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:0000256|HAMAP-Rule:MF_01346"
FT   SITE            373
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   544 AA;  58902 MW;  4D6A594EBCAF24A2 CRC64;
     MAELTISSDE IRSAIANYTS STSAEASREE VGVVTMAADG IAQVSGMPSV MTNELLEFPG
     GVIGVAQNLE TDSIGVVVLG NYESLKEGDE VKRTGDVLSV PVGENFLGRV INPLGQPIDG
     RGDIESTETR ALELQAPSVL QRQPVHEPMQ TGIKAIDAMT PIGRGQRQLI IGDRKTGKTS
     VCIDTILNQR ENWESGDPTK QVRCIYVAIG QKGSTIAALR QTLEEQGALD YTTIVAAPAS
     DSAGFKWLAP FAGAALGQQW MYESKHVLII FDDLTKQAEA YRAISLLLRR PPGREAYPGD
     VFYLHSRLLE RAAKLSDEEG AGSMTALPII ETKANDVGAF IPTNVISITD GQVFLESDLF
     NQGVRPAINV GVSVSRVGGD AQTKGMKKVA GNLRLDLAAY RDLEAFAAFA SDLDEYSKAQ
     LERGERLVEL LKQRETEPQA VEDQMVSIFL AGEGEFDSVA VEDIRRFEAE LWEYLHANNA
     AVYEQINGGT PLSDESKKTL VSATGEFKRS FQSTDGTPVI NEPEAQALAD EDLDQSQITV
     SRKK
//
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