ID   PATS_METJA              Reviewed;         273 AA.
AC   Q58378;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 3.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Soluble P-type ATPase-like phosphatase;
DE            EC=3.6.3.-;
GN   Name=patS; OrderedLocusNames=MJ0968;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=10760521; DOI=10.1016/s0014-5793(00)01374-0;
RA   Ogawa H., Haga T., Toyoshima C.;
RT   "Soluble P-type ATPase from an archaeon, Methanococcus jannaschii.";
RL   FEBS Lett. 471:99-102(2000).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=12753900; DOI=10.1016/s0014-5793(03)00372-7;
RA   Bramkamp M., Gassel M., Herkenhoff-Hesselmann B., Bertrand J.,
RA   Altendorf K.;
RT   "The Methanocaldococcus jannaschii protein Mj0968 is not a P-type ATPase.";
RL   FEBS Lett. 543:31-36(2003).
CC   -!- FUNCTION: Most probably acts as a phosphatase in the cytosol.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- ACTIVITY REGULATION: Inhibited by orthovanadate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius.;
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; L77117; AAB98973.1; -; Genomic_DNA.
DR   PIR; H64420; H64420.
DR   RefSeq; WP_010870482.1; NC_000909.1.
DR   AlphaFoldDB; Q58378; -.
DR   SMR; Q58378; -.
DR   STRING; 243232.MJ_0968; -.
DR   EnsemblBacteria; AAB98973; AAB98973; MJ_0968.
DR   GeneID; 1451866; -.
DR   KEGG; mja:MJ_0968; -.
DR   eggNOG; arCOG01579; Archaea.
DR   HOGENOM; CLU_1052165_0_0_2; -.
DR   InParanoid; Q58378; -.
DR   OMA; GISYCNP; -.
DR   OrthoDB; 66892at2157; -.
DR   PhylomeDB; Q58378; -.
DR   SABIO-RK; Q58378; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Hydrolase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..273
FT                   /note="Soluble P-type ATPase-like phosphatase"
FT                   /id="PRO_0000046397"
FT   ACT_SITE        8
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   273 AA;  30739 MW;  FC6D56FD985E4381 CRC64;
     MKVAIVFDSA GTLVKIMRVI KDLKKNKFIC NSQTVDIVDK KKGRALVIIK EDPLKVVDKE
     NPEKLISDLL KEVEIGISYC NPPINREGIF KDRKTKVKEL QEPLNILKRY EVETGYGSAL
     IIDTYAGEVE YTIATAGCLF KEVKETIKQL KDLGVKVFIA SGDRKGFIKR LAEITGVDER
     YIMAEAHQEL KRDLIRNLKK EGYFTIMVGD GANDVPAMIE SDLAVVTLQN GNVSRRALET
     ADIKIYNIKE IVDICKKVIN GEIKGRMQIK ECS