ID   AMZA_SULAC              Reviewed;         177 AA.
AC   Q4JB73;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Saci_0564;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(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; CP000077; AAY79956.1; -; Genomic_DNA.
DR   RefSeq; WP_011277458.1; NC_007181.1.
DR   AlphaFoldDB; Q4JB73; -.
DR   SMR; Q4JB73; -.
DR   STRING; 330779.Saci_0564; -.
DR   PRIDE; Q4JB73; -.
DR   EnsemblBacteria; AAY79956; AAY79956; Saci_0564.
DR   GeneID; 3473202; -.
DR   KEGG; sai:Saci_0564; -.
DR   PATRIC; fig|330779.12.peg.545; -.
DR   eggNOG; arCOG00458; Archaea.
DR   HOGENOM; CLU_108521_1_0_2; -.
DR   OMA; RSVYDCD; -.
DR   Proteomes; UP000001018; 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..177
FT                   /note="Archaemetzincin"
FT                   /id="PRO_0000159635"
FT   ACT_SITE        130
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         129
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         133
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="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="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01842"
SQ   SEQUENCE   177 AA;  20464 MW;  09EE600ED4AB4DEC CRC64;
     MYKVLLIRLT NLDNLIVNSV RTHLMNMGFE VEVNEEIFHL NAELFNWERW QYNADKLLQL
     VKLTFERYPY DAVIGIGEAD GFSDGLNFVF GLSTKKYGLV FLSRLKEEFY GRVINSSLYI
     ERTLKEVTHE LGHTLGLGHC NNKECVMNFS VSVEDVDKKG KYFCTSCSDK LNINNKS