ID A0A0J6WM74_MYCCU Unreviewed; 451 AA.
AC A0A0J6WM74;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protease 3 {ECO:0000313|EMBL:KMO84475.1};
DE EC=3.4.24.55 {ECO:0000313|EMBL:KMO84475.1};
GN Name=ptrA {ECO:0000313|EMBL:KMO84475.1};
GN ORFNames=MCHUDSM44219_00629 {ECO:0000313|EMBL:KMO84475.1};
OS Mycolicibacterium chubuense (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1800 {ECO:0000313|EMBL:KMO84475.1, ECO:0000313|Proteomes:UP000036176};
RN [1] {ECO:0000313|EMBL:KMO84475.1, ECO:0000313|Proteomes:UP000036176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44219 {ECO:0000313|EMBL:KMO84475.1,
RC ECO:0000313|Proteomes:UP000036176};
RX PubMed=26079817; DOI=10.1093/gbe/evv111;
RA Das S., Pettersson B.M., Behra P.R., Ramesh M., Dasgupta S.,
RA Bhattacharya A., Kirsebom L.A.;
RT "Characterization of Three Mycobacterium spp. with Potential Use in
RT Bioremediation by Genome Sequencing and Comparative Genomics.";
RL Genome Biol. Evol. 7:1871-1886(2015).
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:KMO84475.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYNX01000015; KMO84475.1; -; Genomic_DNA.
DR RefSeq; WP_048416761.1; NZ_UATB01000009.1.
DR AlphaFoldDB; A0A0J6WM74; -.
DR PATRIC; fig|1800.3.peg.632; -.
DR Proteomes; UP000036176; 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:UniProtKB-EC.
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:KMO84475.1};
KW Protease {ECO:0000313|EMBL:KMO84475.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000036176}.
FT DOMAIN 38..184
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 192..368
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48924 MW; 5C34A463E736F877 CRC64;
MPRPPAADAA ALRRVRGGGG TVDKSTAIRR TDLPGGLRVV TEHIPHVHSA SVGVWVNVGS
RDEGRSVAGA AHFLEHLLFK ATPTRTAVQI AQAVDAVGGE LNAFTSREHT CYYAHVLDSD
LALAVDLVAD VVLRGQCFAD DVEIERDVVL EEIAMRDDDP EDTLGDVFLS AMFGDHPVGR
PVIGSVDSIS AMTRTQLHSF HLRRYTPDRM VVAVAGNIDH REVVALVREH FGPRLVRGRS
PVPPRKGAGR VPGRPTLQLV KRDAEQTHLS LGVRTPGRHW EERWALSVLN TALGGGLSSR
LFQQIRETRG LAYSVYSTVD TFADSGALSI YAGCLPERFD EVVRVTTDVL AEVARDGITD
EECRIAKGSL RGGLVLGLED SASRMNRLGR SELNYGQHRT IAETLARIDE VTLDDVNAVA
RQLLARPFGA AVLGPVRGRR SLPRPLQTIA G
//
