ID I4BNU5_MYCCN Unreviewed; 452 AA.
AC I4BNU5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:AFM18952.1};
GN OrderedLocusNames=Mycch_4237 {ECO:0000313|EMBL:AFM18952.1};
OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM18952.1, ECO:0000313|Proteomes:UP000006057};
RN [1] {ECO:0000313|EMBL:AFM18952.1, ECO:0000313|Proteomes:UP000006057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM18952.1,
RC ECO:0000313|Proteomes:UP000006057};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL Submitted (JUN-2012) 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; CP003053; AFM18952.1; -; Genomic_DNA.
DR RefSeq; WP_014817423.1; NC_018027.1.
DR AlphaFoldDB; I4BNU5; -.
DR STRING; 710421.Mycch_4237; -.
DR KEGG; mcb:Mycch_4237; -.
DR PATRIC; fig|710421.3.peg.4232; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_3_4_11; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000006057; 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:AFM18952.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:AFM18952.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006057};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 92..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 365..437
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..87
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 26..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 452 AA; 44777 MW; 597908ABB4820CD1 CRC64;
MTNHPRYSPP PQPGHQPGTH GHMPQGQPAP QRSGSFEQQA YDWRYATEQQ RQAFRSPYDP
YQGAPMPGGP GQYPQPGMPA PQAPRKRSRA GALTAGAVAV AIVSGGIGGG VAMLVHPDHG
APGFSASGAA PSVPAASLPA GSVEQVAAKV VPSVVKLEVD EGRQSEEGSG VILSTDGLIL
TNNHVVASAA SNAPAGPGGP QTKVTFADGR TTSFSIIGTD PGSDIAVVRA KNVSGLTPIA
VGSSAGLRVG QDVVAVGSPL GLEGTVTTGI ISALNRPVAA GGDAQNQNTV LDAIQTDAAI
NPGNSGGALV NMKGELIGIN SAIATMGADS GAAQGGSIGL GFAIPVDQAK RIADELIQSG
SASRASLGVQ VGNNSGGDGA QIVEVTPGGA AAAAGLPNGV VVTKLDDRVI DSADALVAAV
RSKAPGDKVT LTFLDPSGKS QSVDVTLGKA TQ
//
