ID A0A147E719_9MICC Unreviewed; 544 AA.
AC A0A147E719;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=AN277_0208385 {ECO:0000313|EMBL:OAX51502.1}, I6G21_00050
GN {ECO:0000313|EMBL:QPT53660.1};
OS Rothia kristinae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=37923 {ECO:0000313|EMBL:OAX51502.1, ECO:0000313|Proteomes:UP000053171};
RN [1] {ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171};
RA Waterworth S., Matcher G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAX51502.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RUTW2-3 {ECO:0000313|EMBL:OAX51502.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:OAX51502.1, ECO:0000313|Proteomes:UP000053171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuSp02-3 {ECO:0000313|Proteomes:UP000053171}, and RUTW2-3
RC {ECO:0000313|EMBL:OAX51502.1};
RA Waterworth S.C., Walmsley T.A., Matongo T., Davies-Coleman M.T.,
RA Dorrington R.A.;
RT "Identification of putative biosynthetic pathways for the production of
RT bioactive secondary metabolites by the marine actinomycete Kocuria
RT kristinae RUTW2-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:QPT53660.1, ECO:0000313|Proteomes:UP000594975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_864 {ECO:0000313|EMBL:QPT53660.1,
RC ECO:0000313|Proteomes:UP000594975};
RA Sproer C., Gronow S., Severitt S., Schroder I., Tallon L., Sadzewicz L.,
RA Zhao X., Boylan J., Ott S., Bowen H., Vavikolanu K., Mehta A.,
RA Aluvathingal J., Nadendla S., Lowell S., Myers T., Yan Y., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-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 + 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; LJBJ02000017; OAX51502.1; -; Genomic_DNA.
DR EMBL; CP065738; QPT53660.1; -; Genomic_DNA.
DR RefSeq; WP_058730911.1; NZ_NOIV01000001.1.
DR AlphaFoldDB; A0A147E719; -.
DR STRING; 37923.BK826_03550; -.
DR GeneID; 44526259; -.
DR KEGG; rkr:I6G21_00050; -.
DR PATRIC; fig|37923.10.peg.2061; -.
DR Proteomes; UP000053171; Unassembled WGS sequence.
DR Proteomes; UP000594975; 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; 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 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:UP000053171};
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 31..96
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 153..376
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 383..506
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 COMPBIAS 526..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 173..180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
FT SITE 374
FT /note="Required for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346"
SQ SEQUENCE 544 AA; 58873 MW; 0C99AD9ABC5F9BA6 CRC64;
MADLTINADD VRSALNEFAA SYEPGETDRV EVGRVTSAGD GIARVEGLPS VMANELLRFE
DGTLGLAQNL DTRDIGAIVL GDFTGVEEGQ EVHRTGEVLS VPVGDAFLGR VVDPLGHPID
DLGPIESEGR RALELQAPGV TQRKSVHEPL QTGLKAIDAM IPIGRGQRQL IIGDRQTGKT
AIGIDTILNQ KENWETGDPE KQVRCIYVAV GQKASTIASV RQTLEDNGAL EYTTIVASPA
SDAAGFKYLA PYAGSAIGQH WMYGGKHVLI IFDDLSKQAE AYRAVSLLLR RPPGREAYPG
DVFYLHSRLL ERCAKLSDEL GAGSMTGLPI IETKANDVSA FIPTNVISIT DGQIFLQSDL
FNANQRPAVD VGVSVSRVGG AAQIKAMKKV SGTLKLDLAQ YRSMQAFAMF ASDLDEASRR
QLTRGARLTE LLRQPQYTPY NVEDQVAAIW AGTNGHLDDL EVSDVLEFEQ RFLEHLRRNT
SVLTDIASSG KLEDATVEAL KSAVAEVKRD FAAEGPHGGG IQPGHEEHAP VERSEVDQEE
IVKR
//
