ID   AMZA_HALS3              Reviewed;         173 AA.
AC   B0R889;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=OE_4663F;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
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; AM774415; CAP14958.1; -; Genomic_DNA.
DR   RefSeq; WP_010903951.1; NC_010364.1.
DR   AlphaFoldDB; B0R889; -.
DR   SMR; B0R889; -.
DR   EnsemblBacteria; CAP14958; CAP14958; OE_4663F.
DR   GeneID; 5953461; -.
DR   GeneID; 62887827; -.
DR   KEGG; hsl:OE_4663F; -.
DR   HOGENOM; CLU_108521_2_0_2; -.
DR   OMA; RSVYDCD; -.
DR   PhylomeDB; B0R889; -.
DR   Proteomes; UP000001321; 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; Zinc.
FT   CHAIN           1..173
FT                   /note="Archaemetzincin"
FT                   /id="PRO_1000188422"
FT   ACT_SITE        131
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         130
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         134
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         140
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         141
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
SQ   SEQUENCE   173 AA;  19363 MW;  5F84F6AB47AE47C9 CRC64;
     MRVDIVPVGD VPAHVKRQAS SSLRSVYDCE VVVASEQDVP TAAYDEARSQ YRAAEFIDTA
     TRATSGDKTI AITPHDLFYR RRNYVFGLAY LDGRGCVVST YRLQTSSDGG FSNRSSSDVF
     DDRVRKEVVH ELGHTLGLEH CDNNRCAMNF SPTVREVDRK EENLCGSCQR TVF