ID   I0RZT7_MYCXE            Unreviewed;       448 AA.
AC   I0RZT7;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Protease {ECO:0000313|EMBL:EID16640.1};
GN   ORFNames=MXEN_03409 {ECO:0000313|EMBL:EID16640.1};
OS   Mycobacterium xenopi RIVM700367.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID16640.1, ECO:0000313|Proteomes:UP000003584};
RN   [1] {ECO:0000313|EMBL:EID16640.1, ECO:0000313|Proteomes:UP000003584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIVM700367 {ECO:0000313|EMBL:EID16640.1,
RC   ECO:0000313|Proteomes:UP000003584};
RX   PubMed=22628510; DOI=10.1128/JB.00482-12;
RA   Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA   van Soolingen D., Bitter W., Pain A.;
RT   "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL   J. Bacteriol. 194:3282-3283(2012).
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:EID16640.1}.
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DR   EMBL; AJFI01000022; EID16640.1; -; Genomic_DNA.
DR   RefSeq; WP_003919392.1; NZ_AJFI01000022.1.
DR   AlphaFoldDB; I0RZT7; -.
DR   PATRIC; fig|1150591.3.peg.681; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000003584; 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:EID16640.1};
KW   Protease {ECO:0000313|EMBL:EID16640.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003584}.
FT   DOMAIN          35..182
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          189..365
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  48915 MW;  26FD0E876A7C68CC CRC64;
     MPRRPAVNRG ALRRGPHSAE PSAAIRRTTL PGGLRVVTEY LPAVRSASVG VWVGVGSRDE
     GATVAGAAHF LEHLLFKSTP SRTAVDIAQA MDAVGGELNA FTAKEHTCYY AHVLDSDLEL
     AVDLVSDVVL NGRCAAEDVE LERDVVLEEI AMRDDDPEDT LADLFLGALF GDHPVGRPVI
     GTVQSVSAMT RSQLHSFHTR RYTPERMIVA VAGNVDHDEV VGLVREHFGP RLVRGRRPAA
     PRKGAGRING RPRMAVLNRD AEQTHVSLGV RTPGRHWRHR WALSVLHTAL GGGLSSRLFQ
     EVRETRGLAY SVYSSLDIFA DSGALSIYAA CLPERFNDVA QVTCDVLESV ARDGITEAEC
     RIAKGSLRGG LVLGLEDSSS RMNRIGRSEL NYGEHRSIER TLQELDAVTV DEVNSVARRL
     LRRPYGVAVL GPYRSKRAVP QQLRAIVQ
//