AMZA_THEKO
ID AMZA_THEKO Reviewed; 186 AA.
AC Q5JGD6;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=TK1178;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85367.1; -; Genomic_DNA.
DR RefSeq; WP_011250129.1; NC_006624.1.
DR AlphaFoldDB; Q5JGD6; -.
DR SMR; Q5JGD6; -.
DR STRING; 69014.TK1178; -.
DR EnsemblBacteria; BAD85367; BAD85367; TK1178.
DR GeneID; 3235206; -.
DR KEGG; tko:TK1178; -.
DR PATRIC; fig|69014.16.peg.1153; -.
DR eggNOG; arCOG00458; Archaea.
DR HOGENOM; CLU_108521_2_0_2; -.
DR InParanoid; Q5JGD6; -.
DR OMA; RSVYDCD; -.
DR OrthoDB; 72411at2157; -.
DR PhylomeDB; Q5JGD6; -.
DR Proteomes; UP000000536; 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..186
FT /note="Archaemetzincin"
FT /id="PRO_0000159634"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT BINDING 136
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 146
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 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
SQ SEQUENCE 186 AA; 21079 MW; 0ECD7981C8472964 CRC64;
MRVILIVPIG YIPEWLIKDV AEFVDSYYSR RGVSVKAGDS LSESLFLSAY HPFRRQFLGG
AFLPTLSEIG RRAGALATVG ITKVDLYEKG MNFVFGVASE KLRSAVVSIH RLRPEFYGRP
SNDELLIERT VKEVMHELGH VFGLSHCPNV RCVMHFSNSV DDTDIKLPYY CPNCERKLLR
NLEVVL
