ID A0A1A2GDJ8_9MYCO Unreviewed; 510 AA.
AC A0A1A2GDJ8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:OBG27833.1};
GN ORFNames=A5764_02405 {ECO:0000313|EMBL:OBG27833.1};
OS Mycobacterium sp. 852002-51057_SCH5723018.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834094 {ECO:0000313|EMBL:OBG27833.1, ECO:0000313|Proteomes:UP000092171};
RN [1] {ECO:0000313|Proteomes:UP000092171}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=852002-51057_SCH5723018 {ECO:0000313|Proteomes:UP000092171};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Mehaffy C., Tameris M.,
RA Hatherill M., Hanekom W., Mahomed H., Mcshane H.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:OBG27833.1}.
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DR EMBL; LZIR01000035; OBG27833.1; -; Genomic_DNA.
DR RefSeq; WP_067111651.1; NZ_LZIR01000035.1.
DR AlphaFoldDB; A0A1A2GDJ8; -.
DR STRING; 1834094.A5764_02405; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000092171; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:OBG27833.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:OBG27833.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 422..496
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 52568 MW; 43E6ABA2B632B376 CRC64;
MTSDGNDSGN DSGNADARGG QRLAPRPISR PPVDPASRQL FSRPDGLQGS FVAERVRPPK
YRDQSEFAPY DQPADPVLQE AFSRPVGTVD TLQRHPIDSG ALAAERDGAQ TDEADDPWRD
PAAAAALGTP AVAPPAPRTA LGYGGKLGVR DVLFGRKVSY LALGVLLLVA LLIGALGGVI
GNKTAEVVEA FTTSKVTLST GGNTEQPAGR FAKVAAATAG AVVTIESKSD QEGMQGSGVV
IDGRGYIVTN NHVISEAANN PSQFKTTVVF NDGKEVPANL VGRDPKTDLA VLKVDNVDNL
TVARLGDSDK VRVGDEVLAA GSPLGLRSTV THGIISALHR PVPLSGEGSD TDTVIDALQT
DASINHGNSG GPLIDMDSQV IGIDTAGKSL SDSASGLGFA IPINEAKQVA QTLIKDGKIV
HPTLGVSTRS VSNAIASGAQ VANVKAGSPA QKGGMLENDV IVKVGNRNVA DADEFVVAVR
LLTIGQDSPI EVVRDGRHVT LTVKPDPDGG
//
