AMZA_HALWD
ID AMZA_HALWD Reviewed; 173 AA.
AC Q18KE9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=HQ_1374A;
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001;
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA Pfeiffer F., Oesterhelt D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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; AM180088; CAJ51502.1; -; Genomic_DNA.
DR RefSeq; WP_011570657.1; NC_008212.1.
DR AlphaFoldDB; Q18KE9; -.
DR SMR; Q18KE9; -.
DR STRING; 362976.HQ_1374A; -.
DR EnsemblBacteria; CAJ51502; CAJ51502; HQ_1374A.
DR GeneID; 4192283; -.
DR KEGG; hwa:HQ_1374A; -.
DR eggNOG; arCOG00458; Archaea.
DR HOGENOM; CLU_108521_2_0_2; -.
DR OMA; RSVYDCD; -.
DR Proteomes; UP000001975; 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..173
FT /note="Archaemetzincin"
FT /id="PRO_1000070577"
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; 19267 MW; 9592210A20C05379 CRC64;
MLVDIVPIGD LPAQVKREAS AALRGVYECD VTVHEEQSIP DGAFDHSRSQ YRAEQFIELA
SRIGSGEKNI GITAEDLYYR RRNYVFGLAY LNGNGSVIST YRLQTSSDGG LKSKSPDAVF
ADRIRKEVVH EIGHTFGLEH CDNSKCVMSF SPTVREVDVK EENLCGSCNR LLY
