ID L0J1M6_9MYCO Unreviewed; 451 AA.
AC L0J1M6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:AGB25460.1};
GN ORFNames=Mycsm_05262 {ECO:0000313|EMBL:AGB25460.1};
OS Mycobacterium sp. JS623.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB25460.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003078; AGB25460.1; -; Genomic_DNA.
DR RefSeq; WP_015309036.1; NC_019966.1.
DR AlphaFoldDB; L0J1M6; -.
DR STRING; 212767.Mycsm_05262; -.
DR KEGG; msa:Mycsm_05262; -.
DR PATRIC; fig|710686.3.peg.5299; -.
DR HOGENOM; CLU_020120_3_4_11; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000010844; Chromosome.
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 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:AGB25460.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AGB25460.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 364..436
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 44935 MW; EAEC2830BF383CAA CRC64;
MTNHPRYSPP PPPGHRPGGH EQHAAPGYPG APRQYQQPTQ QQPYDWRYAT QQQFRPPYDP
YRGAPQQPPG MPLPPVRQKR SRAGALTAGA LAVAIVSAGI GGGVALLTQP DRPSATSSAT
GLAPSVPAAS LPAGSVEQVA AKVVPSVVKL EVDLGKQSEE GSGIILSSDG LILTNNHVVA
AAKDNPGGPP APVPAGGAQT KVTFADGRTM GFTVVGTDPS SDIAVVRAQG ASGLTPITLG
SSSNLRVGQD VVAVGSPLGL EGTVTTGIIS ALNRPVAAGG DAQNQNTVLD AIQTDAAINP
GNSGGALVNM NGELVGVNSA IATLGGDAGP QAQSGSIGLG FAIPVDQAKR IADELIQSGT
ASHASLGVQV GNDAGVDGAK IVEVTSGGAA AAAGLPSGVV VTKVDDRVIG SADALVAAVR
SKAPGDKVTL TYLDPSGKPQ TVQVTLGKAQ Q
//