VATA_PYRAB
ID VATA_PYRAB Reviewed; 1017 AA.
AC Q9UXU7; G8ZKU4;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=Pab AtpA intein;
DE AltName: Full=Pab VMA intein;
GN Name=atpA; OrderedLocusNames=PYRAB17610; ORFNames=PAB2378;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50666.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71235.1; -; Genomic_DNA.
DR PIR; D75028; D75028.
DR RefSeq; WP_010868880.1; NC_000868.1.
DR AlphaFoldDB; Q9UXU7; -.
DR SMR; Q9UXU7; -.
DR STRING; 272844.PAB2378; -.
DR EnsemblBacteria; CAB50666; CAB50666; PAB2378.
DR GeneID; 1496064; -.
DR KEGG; pab:PAB2378; -.
DR PATRIC; fig|272844.11.peg.1880; -.
DR eggNOG; arCOG00868; Archaea.
DR eggNOG; arCOG03154; Archaea.
DR HOGENOM; CLU_008162_1_0_2; -.
DR OMA; CFAKGTE; -.
DR OrthoDB; 6736at2157; -.
DR PhylomeDB; Q9UXU7; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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; 3.10.28.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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 Pfam; PF14528; LAGLIDADG_3; 2.
DR PRINTS; PR00379; INTEIN.
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 SUPFAM; SSF55608; SSF55608; 1.
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; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW ATP synthesis; ATP-binding; Autocatalytic cleavage; Hydrogen ion transport;
KW Ion transport; Nucleotide-binding; Protein splicing; Translocase;
KW Transport.
FT CHAIN 1..240
FT /note="V-type ATP synthase alpha chain, 1st part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002461"
FT CHAIN 241..669
FT /note="Pab AtpA intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002462"
FT CHAIN 670..1017
FT /note="V-type ATP synthase alpha chain, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002463"
FT DOMAIN 396..529
FT /note="DOD-type homing endonuclease"
SQ SEQUENCE 1017 AA; 114354 MW; 0F2008895F3E407A CRC64;
MVAKGRIIRV TGPLVVADGM KGAKMYEVVR VGELGLIGEI IRLEGDKAVI QVYEETAGVR
PGEPVIGTGS SLSVELGPGL LTSIYDGIQR PLEVIREKTG DFIARGVTAP ALPRDKKWHF
IPKVKVGDKV VGGDIIGEVP ETSIITHKIM VPPGIEGEIV EIAEEGEYTI EEVIAKVKTP
SGEIKELKMY QRWPVRVKRP YKEKLPPEVP LITGQRVIDT FFPQAKGGTA AIPGPFGSGK
CVDGDTLVLT KEFGLIKIKD LYKILDGKGK KTVNGNEEWT ELERPITLYG YKDGKIVEIK
ATHVYKGFSA GMIEIRTRTG RKIKVTPIHK LFTGRVTKNG LEIREVMAKD LKKGDRIIVA
KKIDGGERVK LNIRVEQKRG KKIRIPDVLD EKLAEFLGYL IADGTLKPRT VAIYNNDESL
LRRANELANE LFNIEGKIVK GRTVKALLIH SKALVEFFSK LGVPRNKKAR TWKVPKELLI
SEPEVVKAFI KAYIMCDGYY DENKGEIEIV TASEEAAYGF SYLLAKLGIY AIIREKIIGD
KVYYRVVISG ESNLEKLGIE RVGRGYTSYD IVPVEVEELY NALGRPYAEL KRAGIEIHNY
LSGENMSYEM FRKFAKFVGM EEIAENHLTH VLFDEIVEIR YISEGQEVYD VTTETHNFIG
GNMPTLLHNT VTQHQLAKWS DAQVVIYIGC GERGNEMTDV LEEFPKLKDP KTGKPLMERT
VLIANTSNMP VAAREASIYT GITIAEYFRD MGYDVALMAD STSRWAEALR EISGRLEEMP
GEEGYPAYLA SKLAEFYERA GRVVTLGSDY RVGSVSVIGA VSPPGGDFSE PVVQNTLRVV
KVFWALDADL ARRRHFPAIN WLTSYSLYVD AVKDWWHKNV DPEWKAMRDK AMELLQKESE
LQEIVRIVGP DALPERERAI LLVARMLRED YLQQDAFDEV DTYCPPEKQV TMMRVLLNFY
DKTMEAISRG VPLEEIAKLP VREEIGRMKF EPDVGKIKAL IDKTNEQFEE LFKKYGA
