ID D1AWR5_STRM9 Unreviewed; 588 AA.
AC D1AWR5;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=V-type ATP synthase alpha chain {ECO:0000256|HAMAP-Rule:MF_00309};
DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_00309};
DE AltName: Full=V-ATPase subunit A {ECO:0000256|HAMAP-Rule:MF_00309};
GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_00309};
GN OrderedLocusNames=Smon_0256 {ECO:0000313|EMBL:ACZ00741.1};
OS Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS 9901).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Leptotrichiaceae;
OC Streptobacillus.
OX NCBI_TaxID=519441 {ECO:0000313|EMBL:ACZ00741.1, ECO:0000313|Proteomes:UP000002072};
RN [1] {ECO:0000313|EMBL:ACZ00741.1, ECO:0000313|Proteomes:UP000002072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901
RC {ECO:0000313|Proteomes:UP000002072};
RX PubMed=21304670; DOI=10.4056/sigs.48727;
RA Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA Del Rio T.G., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C.,
RA Ovchinikova G., Pati A., Mavromatis K., Mikhailova N., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Sproer C., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Chain P.;
RT "Complete genome sequence of Streptobacillus moniliformis type strain
RT (9901T).";
RL Stand. Genomic Sci. 1:300-307(2009).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The V-type alpha chain is a catalytic subunit.
CC {ECO:0000256|HAMAP-Rule:MF_00309}.
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_00309};
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_00309}.
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DR EMBL; CP001779; ACZ00741.1; -; Genomic_DNA.
DR AlphaFoldDB; D1AWR5; -.
DR STRING; 519441.Smon_0256; -.
DR KEGG; smf:Smon_0256; -.
DR eggNOG; COG1155; Bacteria.
DR HOGENOM; CLU_008162_3_1_0; -.
DR OrthoDB; 9803053at2; -.
DR Proteomes; UP000002072; Chromosome.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IEA:UniProt.
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 GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR CDD; cd01134; V_A-ATPase_A; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
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; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 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|HAMAP-Rule:MF_00309};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00309}; Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_00309};
KW Hydrolase {ECO:0000313|EMBL:ACZ00741.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00309}; Reference proteome {ECO:0000313|Proteomes:UP000002072};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW Rule:MF_00309};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00309}.
FT DOMAIN 5..67
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 83..200
FT /note="ATPsynthase alpha/beta subunit N-terminal extension"
FT /evidence="ECO:0000259|Pfam:PF16886"
FT DOMAIN 210..433
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT BINDING 230..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00309"
SQ SEQUENCE 588 AA; 65863 MW; 2FA787AF59F4FC5F CRC64;
MQGRIVKVSG PLVVAENMQH ANVFDMVKVG NDKLIGEIIE MRGDRASIQV YEETTGIGTN
EPVETTGMPL SVELGPGLLE NMFDGIQRPL DKIKQRVGDF LLKGVEVNAL DREKIWEFVA
TKSIGDEVSS GYVLGTVQET EVITHKIMVP IGIEGKIKEI KSGNFTVEDT IAVIETVNGD
VNVNMIQRWP VRKGRKYAKK INPDEPLITG QRVIDTFFPV SKGGTACVPG PFGSGKTVVQ
HQFAKWGDAQ VVVYVGCGER GNEMTDVLME FPEIIDPLTG KSLMQRTVLI ANTSNMPVAA
REASIYTGIT IAEYFRDMGY SVSIMADSTS RWAEALREMS GRLEEMPGDE GYPAYLSSRA
ADFYERAGKV VCLGEDERIG ALTVIGAVSP PGGDISEPVS QSTLRIVKVF WGLDAQLAYR
RHFPAINWLN SYSLYQTKVD EWMDKNVDEK FSANRTMAMK LLQEEAGLQE IVRLVGKDTL
SFEDQLKLEA AKSIREDYLQ QNAFHEQDTY TSLDKQNKML NMVLHFYNQA QKALKKNVYV
NDILELEVRE KIARAKYLSE EHIYKIDEIN KEVEEKINEL ISRQGEVM
//
