ID M0BMA4_9EURY Unreviewed; 173 AA.
AC M0BMA4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Archaemetzincin {ECO:0000256|HAMAP-Rule:MF_01842};
DE EC=3.4.-.- {ECO:0000256|HAMAP-Rule:MF_01842};
GN Name=amzA {ECO:0000256|HAMAP-Rule:MF_01842};
GN ORFNames=C479_07081 {ECO:0000313|EMBL:ELZ11607.1};
OS Halovivax asiaticus JCM 14624.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halovivax.
OX NCBI_TaxID=1227490 {ECO:0000313|EMBL:ELZ11607.1, ECO:0000313|Proteomes:UP000011560};
RN [1] {ECO:0000313|EMBL:ELZ11607.1, ECO:0000313|Proteomes:UP000011560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14624 {ECO:0000313|EMBL:ELZ11607.1,
RC ECO:0000313|Proteomes:UP000011560};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is
CC unknown. {ECO:0000256|HAMAP-Rule:MF_01842}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01842};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_01842}.
CC -!- SIMILARITY: Belongs to the peptidase M54 family. {ECO:0000256|HAMAP-
CC Rule:MF_01842}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ11607.1}.
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DR EMBL; AOIQ01000012; ELZ11607.1; -; Genomic_DNA.
DR RefSeq; WP_007699998.1; NZ_AOIQ01000012.1.
DR AlphaFoldDB; M0BMA4; -.
DR STRING; 1227490.C479_07081; -.
DR GeneID; 14375637; -.
DR PATRIC; fig|1227490.4.peg.1440; -.
DR OrthoDB; 50281at2157; -.
DR Proteomes; UP000011560; Unassembled WGS sequence.
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; Collagenase (Catalytic Domain); 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 NCBIfam; NF033823; archmetzin; 1.
DR PANTHER; PTHR15910; ARCHAEMETZINCIN; 1.
DR PANTHER; PTHR15910:SF1; ARCHAEMETZINCIN-2; 1.
DR Pfam; PF07998; Peptidase_M54; 1.
DR PIRSF; PIRSF005785; Zn-prot_arch; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01842};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01842};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01842}; Protease {ECO:0000256|HAMAP-Rule:MF_01842};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_01842}.
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01842"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01842"
SQ SEQUENCE 173 AA; 19163 MW; 684F2FF585475B2A CRC64;
MHVDIVPVGE VSARVKREAS SALRSVYDCD VTIGDGQSIP TGAYDSGRSQ YSAESFIQLA
ERVGRGDKNI AITPQDIFYR RRNYVFGLAY LDGSGSVVST YRLQTSSDGG FSNKSASDIV
DDRIRKEVVH EIGHTYGLEH CNNNRCVMNF SRTVQKVDIK EENLCGSCQR RLG
//
