ID A0A258SVF9_9PROT Unreviewed; 271 AA.
AC A0A258SVF9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=F0F1 ATP synthase subunit alpha {ECO:0000313|EMBL:OYY83189.1};
DE Flags: Fragment;
GN ORFNames=B7Y34_01905 {ECO:0000313|EMBL:OYY83189.1};
OS Methylophilales bacterium 16-45-9.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales.
OX NCBI_TaxID=1970537 {ECO:0000313|EMBL:OYY83189.1, ECO:0000313|Proteomes:UP000216054};
RN [1] {ECO:0000313|EMBL:OYY83189.1, ECO:0000313|Proteomes:UP000216054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-45-9 {ECO:0000313|EMBL:OYY83189.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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|ARBA:ARBA00003784}.
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:OYY83189.1}.
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DR EMBL; NCGQ01000112; OYY83189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258SVF9; -.
DR Proteomes; UP000216054; Unassembled WGS sequence.
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-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 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 InterPro; IPR000793; ATP_synth_asu_C.
DR InterPro; IPR038376; ATP_synth_asu_C_sf.
DR InterPro; IPR005294; ATP_synth_F1_asu.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR027417; P-loop_NTPase.
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 SUPFAM; SSF47917; C-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 4: Predicted;
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023196};
KW CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..133
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 140..265
FT /note="ATP synthase alpha subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00306"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OYY83189.1"
SQ SEQUENCE 271 AA; 29595 MW; 90A6702A6C3D5B50 CRC64;
CTMGEYFRDR GEDALIVYDD LTKQAIAYRQ ISLLLRRPPG REAYPGDVFY IHSRLLERAA
RVNEEYVEKF TNGAVKGKTG SLTALPVIET AAGDVSAFVP TNVISITDGQ IFLETDLFNA
GIRPAINAGI SVSRVGGAAQ TKVIKKLGGG VRLALAQYRE LAAFAQFASD LDEATRKQLD
RGRMFTELMK QAQYAPLSVS NMAITLFAAN KGYFDDVATN KVLAFESKLH GFIASKYKAI
ADAIETSKDL NADNEKALEA AIQDFKATNA Y
//
