ID   J4JUH5_9MYCO            Unreviewed;       524 AA.
AC   J4JUH5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Protease {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MCOL_V220416 {ECO:0000313|EMBL:EJO87297.1};
OS   Mycobacterium colombiense CECT 3035.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1041522 {ECO:0000313|EMBL:EJO87297.1, ECO:0000313|Proteomes:UP000006455};
RN   [1] {ECO:0000313|EMBL:EJO87297.1, ECO:0000313|Proteomes:UP000006455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 3035 {ECO:0000313|EMBL:EJO87297.1,
RC   ECO:0000313|Proteomes:UP000006455};
RX   PubMed=21952541; DOI=10.1128/JB.05928-11;
RA   Gonzalez-Perez M., Murcia M.I., Landsman D., Jordan I.K.,
RA   Marino-Ramirez L.;
RT   "Genome sequence of the Mycobacterium colombiense type strain, CECT 3035.";
RL   J. Bacteriol. 193:5866-5867(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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:EJO87297.1}.
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DR   EMBL; AFVW02000006; EJO87297.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4JUH5; -.
DR   STRING; 1041522.GCA_002105755_00362; -.
DR   eggNOG; COG0596; Bacteria.
DR   Proteomes; UP000006455; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..524
FT                   /note="Protease"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003779212"
FT   DOMAIN          154..309
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          421..522
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          39..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   524 AA;  53240 MW;  F7DF27B6BCB981F9 CRC64;
     MVGMNRPYTC ATILVAVTAL LAGCVPGLAA DPRFATNSGA RPQGVAPSKP APSGPPPIAA
     PKNDLAWHDC TSKVFADAAV PAAAGVRLDC ASYDADLDPV NGGGGTLSIG VVRARSDKTP
     QDAGPLIFTT GSDLPSSAQL PVWLSRAGAD VLATHPIVSV DRRGIGMSSP IDCRDKFDRQ
     QMRDQSQFQT GDDPVANLSE VSNTATTNCG DAVGIGPNAS SYDDAHAASD IERLRSLWDV
     PALALVGIGN GAQVALAYAG SRPDKVARLI LDSPVALGTN AEAAAEQQVK GQQAALDAFA
     AQCIAVNCAL GADPKGAVSA LLADARAGKG PGGVSVAQVA NAITVALGYP VGGRVNATTD
     LANALAGARS GDTNALTNLI NHANAIQDSD GQFVNVCSDA VNRPTPDRVR ELVVAWGKLY
     PDFGTVAALN MVKCVHWPTG SPPPTPKSLK VDVLLLGVQN DPIVGTDGVA ATAASIINAN
     AASKRVMWQG IGHGASIFSG CAVPPLIGYL SSGKLPNTDT YCPA
//