Y555_METJA
ID Y555_METJA Reviewed; 350 AA.
AC Q57975;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative aminopeptidase MJ0555;
DE EC=3.4.11.-;
GN OrderedLocusNames=MJ0555;
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).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250};
CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR EMBL; L77117; AAB98546.1; -; Genomic_DNA.
DR PIR; C64369; C64369.
DR RefSeq; WP_010870059.1; NC_000909.1.
DR AlphaFoldDB; Q57975; -.
DR SMR; Q57975; -.
DR STRING; 243232.MJ_0555; -.
DR EnsemblBacteria; AAB98546; AAB98546; MJ_0555.
DR GeneID; 1451420; -.
DR KEGG; mja:MJ_0555; -.
DR eggNOG; arCOG01518; Archaea.
DR HOGENOM; CLU_047249_1_0_2; -.
DR InParanoid; Q57975; -.
DR OMA; FGWPAIH; -.
DR OrthoDB; 27966at2157; -.
DR PhylomeDB; Q57975; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.40; -; 1.
DR InterPro; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
DR Pfam; PF05343; Peptidase_M42; 1.
DR PIRSF; PIRSF001123; PepA_GA; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome.
FT CHAIN 1..350
FT /note="Putative aminopeptidase MJ0555"
FT /id="PRO_0000071660"
FT ACT_SITE 207
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 350 AA; 38622 MW; 9D4942EF5528955B CRC64;
MSVVEYLKKL SKLHGISGRE DSVREFMKKE LEKYCDSVEI DNFGNLIAKR GNKGKKIMIA
AHMDEIGLMV KYIDDNGFLK FTKIGGIYDP TILNQKVVVH GSKGDLIGVL GSKPPHRMKE
EEKTKIIKYE DMFIDIGAES REEAIEMGVN IGTWVSFLSE VYDLGKNRLT GKAFDDRVGC
AVLLEVMKRL SEEDIDCQVY AVGTVQEEVG LKGARVSAFK INPDVAIALD VTIAGDHPGI
KKEDAPVDLG KGPVVGIVDA SGRGLIAHPK VLDMIKAVSE KYKIDVQWEV GEGGTTDATA
IHLTREGIPT GVISVPARYI HTPVEVIDKR DLEKTVELVY NCIKEVNNFF