ID Q2T0R8_BURTA Unreviewed; 495 AA.
AC Q2T0R8;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:ABC38342.1};
GN OrderedLocusNames=BTH_I0675 {ECO:0000313|EMBL:ABC38342.1};
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS CIP 106301 / E264).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848 {ECO:0000313|EMBL:ABC38342.1, ECO:0000313|Proteomes:UP000001930};
RN [1] {ECO:0000313|EMBL:ABC38342.1, ECO:0000313|Proteomes:UP000001930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264
RC {ECO:0000313|Proteomes:UP000001930};
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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; CP000086; ABC38342.1; -; Genomic_DNA.
DR RefSeq; WP_011401833.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2T0R8; -.
DR KEGG; bte:BTH_I0675; -.
DR HOGENOM; CLU_020120_1_0_4; -.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0042597; C:periplasmic space; 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; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
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; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABC38342.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 290..381
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 407..485
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 246
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 495 AA; 51411 MW; 58DF0FB3C5E6AAA1 CRC64;
MTTRILARGA VAVAVAAALS AGYVAGTRHA EPQIITPAVA ALMPAEAAAK TGIPDFSGLV
ETYGPAVVNI SAKHVVQRVA QRRAAPQLPI DPEDPFYQFF RHFYGQVPGM GGGRQPQPDD
QPSTSLGSGF IISADGYILT NAHVIDGANV VTVKLTDKRE YKAKVVGTDK QSDVAVLKID
ASGLPTVKIG DPAQSKVGQW VVAIGSPYGF DNTVTSGIIS AKSRALPDEN YTPFIQTDVP
VNPGNSGGPL FNLNGEVIGI NSMIYSQTGG FQGLSFAIPI NEAMKVKDEL VKTGHVSRGR
LGVAVQGLNQ TLASSFGLQK PDGALVSSVD PKGPAAKAGL QPGDVILAVD GVPVQDSTTL
PAQIASMKPG TKADLQIWRD KSKKTVSVTL ASLADDQAKA GADEPVEQGR LGVAVRPLLP
RERNGTSLTH GLVVQQSTGP AASAGIQPGD VILAVNGRPV TSAEQLRDAV KRAGNSLALL
IQRDDAQIFV PVDLG
//
