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Database: UniProt
Entry: A0A323VCC5_9ACTN
LinkDB: A0A323VCC5_9ACTN
Original site: A0A323VCC5_9ACTN 
ID   A0A323VCC5_9ACTN        Unreviewed;       545 AA.
AC   A0A323VCC5;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   18-JUN-2025, entry version 24.
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   ORFNames=DMO24_05535 {ECO:0000313|EMBL:PZA22355.1}, FHX36_004334
GN   {ECO:0000313|EMBL:MBB3678545.1};
OS   Modestobacter versicolor.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=429133 {ECO:0000313|EMBL:PZA22355.1, ECO:0000313|Proteomes:UP000247602};
RN   [1] {ECO:0000313|EMBL:PZA22355.1, ECO:0000313|Proteomes:UP000247602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CP153-2 {ECO:0000313|EMBL:PZA22355.1,
RC   ECO:0000313|Proteomes:UP000247602};
RA   Gundlapally S.R.;
RT   "Draft genome sequence of Modestobacter versicolor CP153-2.";
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB3678545.1, ECO:0000313|Proteomes:UP000580718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16678 {ECO:0000313|EMBL:MBB3678545.1,
RC   ECO:0000313|Proteomes:UP000580718};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
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 + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out);
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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PZA22355.1}.
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DR   EMBL; JACIBU010000002; MBB3678545.1; -; Genomic_DNA.
DR   EMBL; QKNV01000036; PZA22355.1; -; Genomic_DNA.
DR   RefSeq; WP_110551342.1; NZ_JACIBU010000002.1.
DR   AlphaFoldDB; A0A323VCC5; -.
DR   OrthoDB; 9803053at2; -.
DR   Proteomes; UP000247602; Unassembled WGS sequence.
DR   Proteomes; UP000580718; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProtKB-KW.
DR   GO; GO:0043531; F:ADP binding; IEA:TreeGrafter.
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   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   FunFam; 1.20.150.20:FF:000001; ATP synthase subunit alpha; 1.
DR   FunFam; 3.40.50.300:FF:000002; ATP synthase subunit alpha; 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   NCBIfam; NF009884; PRK13343.1; 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   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:UP000247602};
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   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   545 AA;  58901 MW;  BE86348326289A4E CRC64;
     MAELTISADE IRSAIQNYVT DYTPDVSREE VGVVTEAGDG IARVEGLPSV MTNELLEFEG
     GVRGLALNLD VREVGVVILG DFAGIEEGQT VRRTGEVLSV AVGDGYLGRV VDPLGNPIDG
     AGPIETTSRR ALELQAPTVV QRQSVHEPMQ TGIKAIDAMT PIGRGQRQLI IGDRQTGKSA
     IALDTIINQK QAWATGDPSQ QVRCIYVAVG QKGSTIAATR AALEDAGAME YTTIVAAPAS
     EPAGFKYIAP YTGSAIGQHW MYEGKHVLIV FDDLSKQAEA YRAVSLLLRR PPGREAYPGD
     VFYLHSRLLE RCAKLSDELG AGSMTGLPLI ETKGNDVSAY IPTNVISITD GQIFLETGLF
     NSGVRPAINV GVSVSRVGGS AQIKAMKSVA GRLRLDLAQF RELEAFASFS SDLDASSRAT
     LDRGQRLVEL LKQGQYSPFP VEREVVSLWL GTTGKLDRVP VPDVRRFESE FLEFIGRGDN
     PIFDTIRESK KLDDDTVGSL ERAVETFYGQ FTTSDGESLQ VRDEAVEAMD AKDRGQETVQ
     VKRSA
//
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