ID   A0A0U1PTI9_9MICO        Unreviewed;       452 AA.
AC   A0A0U1PTI9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:KKM45854.1};
GN   ORFNames=VT73_05450 {ECO:0000313|EMBL:KKM45854.1};
OS   Rathayibacter toxicus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Rathayibacter.
OX   NCBI_TaxID=145458 {ECO:0000313|EMBL:KKM45854.1, ECO:0000313|Proteomes:UP000052979};
RN   [1] {ECO:0000313|EMBL:KKM45854.1, ECO:0000313|Proteomes:UP000052979}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FH142 {ECO:0000313|EMBL:KKM45854.1,
RC   ECO:0000313|Proteomes:UP000052979};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Luster D.G., Sechler A.J., Schneider W.L., Winegar R.A.;
RT   "Draft genome sequence of Rathayibacter toxicus strain FH-142 (AKA 70134 or
RT   CS 32), a Western Australian isolate.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KKM45854.1}.
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DR   EMBL; LBFI01000031; KKM45854.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0U1PTI9; -.
DR   STRING; 145458.APU90_02055; -.
DR   PATRIC; fig|145458.8.peg.1230; -.
DR   eggNOG; COG0612; Bacteria.
DR   Proteomes; UP000052979; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KKM45854.1};
KW   Protease {ECO:0000313|EMBL:KKM45854.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052979}.
FT   DOMAIN          21..180
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          187..369
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   452 AA;  47733 MW;  8BCEB7D4CED1B9F1 CRC64;
     MTIRAAGGSL VRRSVLSSGV RILSEEVPGA RSVTVGFWVA AGSRDEQPGR PSVAGASAVP
     SNFGSTHFLE HLLFKGTRSR SALDIAVSFD SVGGEHNALT AKEHTCYYAK IQDRDLSMAV
     EVIADMVTSS RIDADEFETE RGVILEELAM ADDDPADVAS ERLFEAVFGE HPLGRPIGGT
     AATIREATRD AVWSHYRAAY RPCDLVVSVA GAVDHNELVS ALERVLAADG WDLKTPASPV
     ARRVGGSANF TRGTALSVVH RPTEQANLFI GVPGIAAGDE RRMTMGVLNS ILGGGMSSRL
     FQEVREKRGL AYSVYSFAPS YSDAGLFGLY AACAPSKAGT VAELLLAEFR RLADGGVSPT
     ELSRAQGQLS GAAALALEDS DMRMSRLARA ELTFGEFVDL DESLRRLARV NVEDVQDLAA
     ALAAGPASIS VVGAVDESTF AAISEKESAP AI
//