ID D2RQI7_HALTV Unreviewed; 173 AA.
AC D2RQI7;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
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 OrderedLocusNames=Htur_3502 {ECO:0000313|EMBL:ADB62364.1};
OS Haloterrigena turkmenica (strain ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB
OS 13204 / VKM B-1734 / 4k) (Halococcus turkmenicus).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Haloterrigena.
OX NCBI_TaxID=543526 {ECO:0000313|EMBL:ADB62364.1, ECO:0000313|Proteomes:UP000001903};
RN [1] {ECO:0000313|EMBL:ADB62364.1, ECO:0000313|Proteomes:UP000001903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51198 / DSM 5511 / JCM 9101 / NCIMB 13204 / VKM B-1734 /
RC 4k {ECO:0000313|Proteomes:UP000001903};
RX PubMed=21304683; DOI=10.4056/sigs.681272;
RA Saunders E., Tindall B.J., Fahnrich R., Lapidus A., Copeland A.,
RA Del Rio T.G., Lucas S., Chen F., Tice H., Cheng J.F., Han C., Detter J.C.,
RA Bruce D., Goodwin L., Chain P., Pitluck S., Pati A., Ivanova N.,
RA Mavromatis K., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Haloterrigena turkmenica type strain (4k).";
RL Stand. Genomic Sci. 2:107-116(2010).
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}.
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DR EMBL; CP001860; ADB62364.1; -; Genomic_DNA.
DR RefSeq; WP_012944620.1; NC_013743.1.
DR AlphaFoldDB; D2RQI7; -.
DR STRING; 543526.Htur_3502; -.
DR GeneID; 8744122; -.
DR KEGG; htu:Htur_3502; -.
DR eggNOG; arCOG00458; Archaea.
DR HOGENOM; CLU_108521_2_0_2; -.
DR OrthoDB; 50281at2157; -.
DR Proteomes; UP000001903; 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; 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; 19200 MW; 34B4BD26AD22874A CRC64;
MLVDIVPVGN VPANVKRAAS AALRSVYDCD VSVNDSQSVP NGAYDADRNQ YAAETFIQLA
ERVGRGTKNI AITPHDLFYR RRNYVFGLAY LDGSGSVVST YRLQTSSDGG FSNQSAEDIF
EDRVRKEIVH EIGHTYGLEH CDNNRCVMNF SPTVREVDIK EENLCGSCQR LIS
//
