VATA_THEAC
ID VATA_THEAC Reviewed; 764 AA.
AC Q9P997; Q9HM65;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=V-type ATP synthase alpha chain;
DE EC=7.1.2.2;
DE AltName: Full=V-ATPase subunit A;
DE Contains:
DE RecName: Full=Tac AtpA intein;
DE AltName: Full=Tac VMA intein;
GN Name=atpA; OrderedLocusNames=Ta0004;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11722801; DOI=10.1186/1471-2091-2-13;
RA Senejani A.G., Hilario E., Gogarten J.P.;
RT "The intein of the Thermoplasma A-ATPase A subunit: structure, evolution
RT and expression in E. coli.";
RL BMC Biochem. 2:13-13(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The archaeal alpha chain is a catalytic subunit.
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 -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the VDE intervening region (intein)
CC followed by peptide ligation. {ECO:0000305}.
CC -!- MISCELLANEOUS: The intein interrupts the ATP-binding site.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000305}.
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DR EMBL; AJ292523; CAB99208.1; -; mRNA.
DR EMBL; AF286477; AAF88065.1; -; mRNA.
DR EMBL; AB045977; BAB00608.1; -; mRNA.
DR EMBL; AL445063; CAC11153.1; -; Genomic_DNA.
DR RefSeq; WP_010900431.1; NC_002578.1.
DR AlphaFoldDB; Q9P997; -.
DR SMR; Q9P997; -.
DR STRING; 273075.Ta0004; -.
DR EnsemblBacteria; CAC11153; CAC11153; CAC11153.
DR GeneID; 1455676; -.
DR KEGG; tac:Ta0004; -.
DR eggNOG; arCOG00868; Archaea.
DR HOGENOM; CLU_008162_1_1_2; -.
DR OMA; CFAKGTE; -.
DR OrthoDB; 6736at2157; -.
DR Proteomes; UP000001024; Chromosome.
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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 2.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 2: Evidence at transcript level;
KW ATP synthesis; ATP-binding; Autocatalytic cleavage; Hydrogen ion transport;
KW Ion transport; Nucleotide-binding; Protein splicing; Reference proteome;
KW Translocase; Transport.
FT CHAIN 1..235
FT /note="V-type ATP synthase alpha chain, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002470"
FT CHAIN 236..409
FT /note="Tac AtpA intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002471"
FT CHAIN 410..764
FT /note="V-type ATP synthase alpha chain, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002472"
FT CONFLICT 201..204
FT /note="PPEI -> LSRD (in Ref. 1; CAB99208/AAF88065)"
FT /evidence="ECO:0000305"
FT CONFLICT 209..216
FT /note="GQRVIDAL -> AQSGNRCA (in Ref. 1; CAB99208)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..226
FT /note="KGGTAA -> EAANCR (in Ref. 1; CAB99208/AAF88065)"
FT /evidence="ECO:0000305"
FT CONFLICT 261..267
FT /note="QDQKNAV -> RPKERG (in Ref. 1; CAB99208/AAF88065)"
FT /evidence="ECO:0000305"
FT CONFLICT 281..282
FT /note="PL -> SW (in Ref. 1; CAB99208/AAF88065)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="S -> T (in Ref. 1; CAB99208/AAF88065/BAB00608)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="T -> N (in Ref. 1; CAB99208/AAF88065/BAB00608)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..352
FT /note="CA -> WP (in Ref. 1; CAB99208/AAF88065)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..462
FT /note="DRTVL -> TGLSF (in Ref. 1; CAB99208/AAF88065)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 764 AA; 84825 MW; F1CF0EF37770306E CRC64;
MGKIIRISGP VVVAEDVEDA KMYDVVKVGE MGLIGEIIKI EGNRSTIQVY EDTAGIRPDE
KVENTRRPLS VELGPGILKS IYDGIQRPLD VIKITSGDFI ARGLNPPALD RQKKWEFVPA
VKKGETVFPG QILGTVQETS LITHRIMVPE GISGKVTMIA DGEHRVEDVI ATVSGNGKSY
DIQMMTTWPV RKARRVQRKL PPEIPLVTGQ RVIDALFPVA KGGTAAVPGP FGSGKCVSGD
TPVLLDAGER RIGDLFMEAI QDQKNAVEIG QNEEIVRLHD PLRIYSMVGS EIVESVSHAI
YHGKSNAIVT VRTENGREVR VTPVHKLFVK IGNSVIERPA SEVNEGDEIA CASVSENGDS
QTVTTTLVLT FDRVVSKEMH SGVFDVYDLM VPDYGYNFIG GNGLIVLHNT VIQHQLAKWS
DANIVVYIGC GERGNEMTEI LTTFPELKDP NTGQPLMDRT VLIANTSNMP VAAREASIYT
GITIAEYYRD MGYDVALMAD STSRWAEALR EISGRLEEMP GEEGYPAYLG RRVSEFYERS
GRARLVSPDE RYGSITVIGA VSPPGGDISE PVSQNTLRVT RVFWALDAAL ANRRHFPSIN
WLNSYSLYTE DLRSWYDKNV SSEWSALRER AMEILQRESE LQEVAQLVGY DAMPEKEKSI
LDVARIIRED FLQQSAFDEI DAYCSLKKQY LMLKAIMEID TYQNKALDSG ATMDNLASLA
VREKLSRMKI VPEAQVESYY NDLVEEIHKE YGNFIGEKNA EASL
