ID   A0A1B9CMI0_MYCMA        Unreviewed;       451 AA.
AC   A0A1B9CMI0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Zinc protease {ECO:0000313|EMBL:OCB43497.1};
GN   ORFNames=A5677_06350 {ECO:0000313|EMBL:OCB43497.1};
OS   Mycobacterium malmoense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1780 {ECO:0000313|EMBL:OCB43497.1, ECO:0000313|Proteomes:UP000092683};
RN   [1] {ECO:0000313|EMBL:OCB43497.1, ECO:0000313|Proteomes:UP000092683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E3012 {ECO:0000313|EMBL:OCB43497.1,
RC   ECO:0000313|Proteomes:UP000092683};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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:OCB43497.1}.
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DR   EMBL; MBEE01000254; OCB43497.1; -; Genomic_DNA.
DR   RefSeq; WP_065440727.1; NZ_MBEE01000254.1.
DR   AlphaFoldDB; A0A1B9CMI0; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000092683; 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:OCB43497.1};
KW   Protease {ECO:0000313|EMBL:OCB43497.1}.
FT   DOMAIN          38..185
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          191..368
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   451 AA;  48931 MW;  8F13554A7461ED0B CRC64;
     MPRPRAADRA AALRRGKHTL EVETSTALRR STLPGGLRVV TEYLPSVRSA SVGVWVGVGS
     RDEGATVAGA AHFLEHLLFK STPTRSAVDI AQAMDAVGGE LNAFTAKEHT CYYAHVLDSD
     LALAVDLVAD VVLNGRCAAD DVELERDVVL EEIAMRDDDP EDALGDMFLG AMFGDHPVGR
     PVIGTAQSVS SMTRTQLHSF HVRRYTPERM VVAVAGNVDH DEVVALVRAH FGPHLVRGRR
     PIAPRKGAGR VTGRPGLMLG NRDAEQTHVS LGVRTPGRGW RHRWALSVLH SALGGGLSSR
     LFQEVRELRG LAYSVYSTVD IFADSGALSV YAACQPERFA EVMKVTNEVL ESVARDGITE
     AECRIAKGSL RGGLVLGLED SSSRMSRLGR NELNYGEHRS IEHTLRKIDE VTVEEVNAVA
     RRLLSQPYGA AVLGPYASKR SLPQQLRAMV N
//