ID L0EHZ2_THECK Unreviewed; 523 AA.
AC L0EHZ2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Trypsin-like serine protease with C-terminal PDZ domain {ECO:0000313|EMBL:AGA58790.1};
GN OrderedLocusNames=Theco_2700 {ECO:0000313|EMBL:AGA58790.1};
OS Thermobacillus composti (strain DSM 18247 / JCM 13945 / KWC4).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Thermobacillus.
OX NCBI_TaxID=717605 {ECO:0000313|EMBL:AGA58790.1, ECO:0000313|Proteomes:UP000010795};
RN [1] {ECO:0000313|Proteomes:UP000010795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18247 / JCM 13945 / KWC4
RC {ECO:0000313|Proteomes:UP000010795};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Anderson I.,
RA Woyke T.;
RT "Complete sequence of chromosome of Thermobacillus composti KWC4.";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003255; AGA58790.1; -; Genomic_DNA.
DR RefSeq; WP_015255532.1; NC_019897.1.
DR AlphaFoldDB; L0EHZ2; -.
DR STRING; 717605.Theco_2700; -.
DR KEGG; tco:Theco_2700; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_0_2_9; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000010795; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 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:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AGA58790.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010795};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 423..505
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 55419 MW; D336792A216B4114 CRC64;
MDDKNNVNRP YDDFFRRPEE RSGLNGRAGE EGSGAADGGA ADAAGGTAAK PVYYYSYGPF
RSGGTDRDAS DAEPVIRHEA AAAERIDAGT AARPAPAVRT WTVRERRRGS WWAPVAAFLA
GILLTGSLMI ASDRLNLFTG SDQALAQSPS AGGAANPGAA PEGSTAAGSS GGKVSNAVDL
VRPNNIAKIV EQSSPAVVKI ETYVKTRSRS GNSLFDDPFF RQFFGDSYRI PTDDEGSQQL
RPSGLGSGFF FDKEGYILTN QHVVGGADQI MVTVIGYDEP FEAELLGSSY DLDLAVLKIK
GDKDFPTLPL GDSDTINVGE WVVAIGNPNG FDHTVTVGVL SAKERPITIQ DTEGTRQYQH
LLQTDASINP GNSGGPLINL AGEVIGINTA VSTTAQGIGF AIPTSTIVGV LDTLKENKPV
PQPFIGATLA DITEQAASQL GLDNTKGSIV VNILYNSPAY KADLRQYDVI VGMDGKKYDT
KEDLIKAIQN KKVGEKAVLD VIRGGNQVQI TVEIGDKNDF NVQ
//
