VATA_PYRHO
ID VATA_PYRHO Reviewed; 964 AA.
AC O57728;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
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=Endonuclease PI-Pho2;
DE EC=3.1.-.-;
DE AltName: Full=Pho AtpA intein;
DE AltName: Full=Pho VMA intein;
GN Name=atpA; OrderedLocusNames=PH1975;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000001; BAA31102.1; -; Genomic_DNA.
DR PIR; G71213; G71213.
DR RefSeq; WP_010886039.1; NC_000961.1.
DR PDB; 1VDZ; X-ray; 2.55 A; A=1-964.
DR PDB; 3I4L; X-ray; 2.40 A; A=1-964.
DR PDB; 3I72; X-ray; 2.47 A; A=1-964.
DR PDB; 3I73; X-ray; 2.40 A; A=1-964.
DR PDB; 3IKJ; X-ray; 2.40 A; A=1-964.
DR PDB; 3M4Y; X-ray; 2.38 A; A=1-964.
DR PDB; 3MFY; X-ray; 2.35 A; A=1-964.
DR PDB; 3ND8; X-ray; 2.40 A; A=1-964.
DR PDB; 3ND9; X-ray; 3.10 A; A=1-964.
DR PDB; 3P20; X-ray; 2.85 A; A=1-964.
DR PDB; 3QG1; X-ray; 2.95 A; A=1-238, A=617-964.
DR PDB; 3QIA; X-ray; 2.60 A; A=1-964.
DR PDB; 3QJY; X-ray; 2.35 A; A=1-964.
DR PDB; 3SDZ; X-ray; 2.53 A; A=1-964.
DR PDB; 3SE0; X-ray; 2.62 A; A=1-964.
DR PDB; 5X09; X-ray; 2.35 A; A=51-964.
DR PDBsum; 1VDZ; -.
DR PDBsum; 3I4L; -.
DR PDBsum; 3I72; -.
DR PDBsum; 3I73; -.
DR PDBsum; 3IKJ; -.
DR PDBsum; 3M4Y; -.
DR PDBsum; 3MFY; -.
DR PDBsum; 3ND8; -.
DR PDBsum; 3ND9; -.
DR PDBsum; 3P20; -.
DR PDBsum; 3QG1; -.
DR PDBsum; 3QIA; -.
DR PDBsum; 3QJY; -.
DR PDBsum; 3SDZ; -.
DR PDBsum; 3SE0; -.
DR PDBsum; 5X09; -.
DR AlphaFoldDB; O57728; -.
DR SMR; O57728; -.
DR STRING; 70601.3258419; -.
DR EnsemblBacteria; BAA31102; BAA31102; BAA31102.
DR GeneID; 1442821; -.
DR KEGG; pho:PH1975; -.
DR eggNOG; arCOG00868; Archaea.
DR eggNOG; arCOG03154; Archaea.
DR OMA; CFAKGTE; -.
DR OrthoDB; 6736at2157; -.
DR BRENDA; 7.1.2.2; 5244.
DR EvolutionaryTrace; O57728; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease 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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
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; -; 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; IPR027434; Homing_endonucl.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; Autocatalytic cleavage;
KW Endonuclease; Hydrogen ion transport; Hydrolase; Intron homing;
KW Ion transport; Nuclease; 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_0000002467"
FT CHAIN 241..616
FT /note="Endonuclease PI-Pho2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002468"
FT CHAIN 617..964
FT /note="V-type ATP synthase alpha chain, 2nd part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002469"
FT DOMAIN 392..518
FT /note="DOD-type homing endonuclease"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:3QIA"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:3M4Y"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:3QJY"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:3QJY"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3QJY"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3QJY"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3I4L"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3QJY"
FT HELIX 617..626
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 630..636
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 639..642
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 643..650
FT /evidence="ECO:0007829|PDB:3MFY"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:3MFY"
FT TURN 657..659
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 663..666
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 674..676
FT /evidence="ECO:0007829|PDB:3QJY"
FT HELIX 678..697
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:3MFY"
FT TURN 709..711
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 713..719
FT /evidence="ECO:0007829|PDB:3SE0"
FT HELIX 735..744
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 748..751
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 753..756
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 759..767
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 771..775
FT /evidence="ECO:0007829|PDB:3QJY"
FT HELIX 779..786
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 795..799
FT /evidence="ECO:0007829|PDB:3MFY"
FT TURN 808..810
FT /evidence="ECO:0007829|PDB:3MFY"
FT STRAND 812..814
FT /evidence="ECO:0007829|PDB:3M4Y"
FT HELIX 816..826
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 831..855
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 857..859
FT /evidence="ECO:0007829|PDB:3ND9"
FT HELIX 862..877
FT /evidence="ECO:0007829|PDB:3MFY"
FT TURN 886..889
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 893..915
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 920..924
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 927..932
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 933..937
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 941..945
FT /evidence="ECO:0007829|PDB:3MFY"
FT HELIX 947..962
FT /evidence="ECO:0007829|PDB:3MFY"
SQ SEQUENCE 964 AA; 107855 MW; 33252C47713BD5E1 CRC64;
MVAKGRIIRV TGPLVVADGM KGAKMYEVVR VGELGLIGEI IRLEGDKAVI QVYEETAGVR
PGEPVVGTGA SLSVELGPGL LTSIYDGIQR PLEVIREKTG DFIARGVTAP ALPRDKKWHF
IPKAKVGDKV VGGDIIGEVP ETSIIVHKIM VPPGIEGEIV EIAEEGDYTI EEVIAKVKTP
SGEIKELKMY QRWPVRVKRP YKEKLPPEVP LITGQRVIDT FFPQAKGGTA AIPGPFGSGK
CVDGDTLVLT KEFGLIKIKE LYEKLDGKGR KIVEGNEEWT ELEKPITVYG YKDGKIVEIK
ATHVYKGVSS GMVEIRTRTG RKIKVTPIHR LFTGRVTKDG LILKEVMAMH VKPGDRIAVV
KKIDGGEYIK LDSSNVGEIK VPEILNEELA EFLGYLMANG TLKSGIIEIY CDDESLLERV
NSLSLKLFGV GGRIVQKVDG KALVIQSKPL VDVLRRLGVP EDKKVENWKV PRELLLSPSN
VVRAFVNAYI KGKEEVEITL ASEEGAYELS YLFAKLGIYV TISKSGEYYK VRVSRRGNLD
TIPVEVNGMP KVLPYEDFRK FAKSIGLEEV AENHLQHIIF DEVIDVRYIP EPQEVYDVTT
ETHNFVGGNM PTLLHNTVTQ HQLAKWSDAQ VVIYIGCGER GNEMTDVLEE FPKLKDPKTG
KPLMERTVLI ANTSNMPVAA REASIYTGIT IAEYFRDMGY DVALMADSTS RWAEALREIS
GRLEEMPGEE GYPAYLASKL AEFYERAGRV VTLGSDYRVG SVSVIGAVSP PGGDFSEPVV
QNTLRVVKVF WALDADLARR RHFPAINWLT SYSLYVDAVK DWWHKNIDPE WKAMRDKAMA
LLQKESELQE IVRIVGPDAL PERERAILLV ARMLREDYLQ QDAFDEVDTY CPPEKQVTMM
RVLLNFYDKT MEAINRGVPL EEIAKLPVRE EIGRMKFERD VSKIRSLIDK TNEQFEELFK
KYGA