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Database: UniProt
Entry: H0E4H6_9ACTN
LinkDB: H0E4H6_9ACTN
Original site: H0E4H6_9ACTN 
ID   H0E4H6_9ACTN            Unreviewed;       518 AA.
AC   H0E4H6;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   13-SEP-2023, entry version 52.
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=PAI11_17070 {ECO:0000313|EMBL:EHN11428.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN11428.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN11428.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN11428.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
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}.
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:EHN11428.1}.
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DR   EMBL; AGUD01000106; EHN11428.1; -; Genomic_DNA.
DR   RefSeq; WP_007573314.1; NZ_AGUD01000106.1.
DR   AlphaFoldDB; H0E4H6; -.
DR   PATRIC; fig|1097667.3.peg.1690; -.
DR   OrthoDB; 9803053at2; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
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:EHN11428.1};
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:UP000005143};
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          28..93
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02874"
FT   DOMAIN          150..365
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          372..496
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
FT   SITE            363
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   518 AA;  55735 MW;  2E0D2AB066523FF3 CRC64;
     MQIKPDEITS ILRSRIEGLD AGKAELNEVG TVLSVSDGIA RIHGLDNAVS FEQLELPHGV
     TGLALNLDAD NVGAVLFGDW EKIVEGDTVK RTGTQLEIPV GDALLGRIVS PLGVPLDGKG
     PIETTETRPL EVKAPGIIER QPVEEPLQTG IKAIDAMIPI GRGQRELIIG DRQTGKTSIA
     VDAIINNKDA GVISVYVAIG QRMATVVNLA QVLAENGALD SAIIVAAGAD EAAPIKYIAP
     YAGAAMAEHF VYNGGHTLAV YDDLTKHAFA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAVKLSDALG GGSMTALPII ETQAGDVSAY IPTNVISITD GQIFLEPKLF YSGVRPAINV
     GISVSRVGSS AQVKPMKKVA GRIKTELSQF RDLEAFAQFG SDLDADTRRT LARGERLVKT
     LNQGERSPVP VEDQVIQIYA ATNGYVDRIS ADRVEEFHLR LTETAHSEIP QLREKIRGGD
     WSDETVAGVK AFVAKFAEED FGYDLDEDGE PLQQAVTA
//
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