ID   AMZA_METJA              Reviewed;         179 AA.
AC   Q57729;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Archaemetzincin {ECO:0000255|HAMAP-Rule:MF_01842};
DE            EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_01842};
GN   Name=amzA {ECO:0000255|HAMAP-Rule:MF_01842}; OrderedLocusNames=MJ0281;
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   -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
CC       unknown. {ECO:0000255|HAMAP-Rule:MF_01842}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01842};
CC       Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the
CC       other seems to have a structural role. {ECO:0000255|HAMAP-
CC       Rule:MF_01842};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01842}.
CC   -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000255|HAMAP-
CC       Rule:MF_01842}.
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DR   EMBL; L77117; AAB98269.1; -; Genomic_DNA.
DR   PIR; B64335; B64335.
DR   AlphaFoldDB; Q57729; -.
DR   SMR; Q57729; -.
DR   STRING; 243232.MJ_0281; -.
DR   MEROPS; M54.001; -.
DR   EnsemblBacteria; AAB98269; AAB98269; MJ_0281.
DR   KEGG; mja:MJ_0281; -.
DR   eggNOG; arCOG00458; Archaea.
DR   HOGENOM; CLU_108521_2_0_2; -.
DR   InParanoid; Q57729; -.
DR   OMA; KDRGQYH; -.
DR   PhylomeDB; Q57729; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   CDD; cd11375; Peptidase_M54; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   HAMAP; MF_01842; Archaemetzincin; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR012962; Pept_M54_archaemetzincn.
DR   InterPro; IPR012091; Pept_M54_archaemetzncn_arc/bac.
DR   PANTHER; PTHR15910; PTHR15910; 1.
DR   Pfam; PF07998; Peptidase_M54; 1.
DR   PIRSF; PIRSF005785; Zn-prot_arch; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW   Zinc.
FT   CHAIN           1..179
FT                   /note="Archaemetzincin"
FT                   /id="PRO_0000159626"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         128
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         144
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         163
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         166
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
SQ   SEQUENCE   179 AA;  20514 MW;  895A7E935A757CE8 CRC64;
     MVMIMRICIQ PVGDVNDEIL KFLKKKFGEV FGMCEILPKI DIPIYAYNFS RGQFNSTLIL
     KSLPTVEDIV LGVTEVDIYA DNLNFVFGEA ELFGKRALIS LARLRPEFYG LPPNKDVLKI
     RALKEAIHEI GHVLGLIHCE NKRCVMSFSN SIIDVDLKDW RYCKKCLKKL QDRGIYISI