ID A0A069PRN2_9BURK Unreviewed; 513 AA.
AC A0A069PRN2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Serine peptidase {ECO:0000313|EMBL:KDR43092.1};
GN ORFNames=BG61_02175 {ECO:0000313|EMBL:KDR43092.1};
OS Caballeronia glathei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR43092.1, ECO:0000313|Proteomes:UP000027466};
RN [1] {ECO:0000313|EMBL:KDR43092.1, ECO:0000313|Proteomes:UP000027466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR43092.1,
RC ECO:0000313|Proteomes:UP000027466};
RA Liu X.Y., Li C.X., Xu J.H.;
RT "Draft Genome Sequences of Four Burkholderia Strains.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:KDR43092.1}.
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; JFHC01000010; KDR43092.1; -; Genomic_DNA.
DR RefSeq; WP_035925403.1; NZ_JFHC01000010.1.
DR AlphaFoldDB; A0A069PRN2; -.
DR STRING; 60547.GCA_000751215_00532; -.
DR Proteomes; UP000027466; Unassembled WGS sequence.
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; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR043504; Peptidase_S1_PA_chymotrypsin.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000027466};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010593673"
FT DOMAIN 307..363
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 410..498
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 89..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 251
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 513 AA; 53168 MW; 77026008C61111CB CRC64;
MSNSSLRRFF AAAALAVCLP FLSNTAAAVT PTVNLPDFTT LVDKVGPSVV NIRTTSRVGT
SSDLRGLPPG LDDGDMSEFF RRFFGIPMPN QPGVPRGGGG GGGGGGGDGG KGGGGRGAPP
DDSQDNSEQS SGVGSGFILS TDGYVMTNAH VVDDADTIYV TLTDKREFKA RLVGVDERTD
VAVVKINASN LPAITIGDSN KVRVGEWVLA IGSPFGLDNT VTAGIVSAKG RDTGDYLPFI
QTDVAVNPGN SGGPLINMAG EVIGINSQIY SRTGGFMGIS FAIPIDEAMR VADQLKTVGK
VVRGRIAVAI GEVTKDVADS LGLPKAQGAL VSSVEAGGPA DKAGVQPGDI ILKFNGHNVE
TATDLPRMVG DSKPGSKATV TVWRKGQTRD LPITIAEMQP DKVARAEQRK TPAPKERASN
SLGMAVSDIP ADQKKALKLT GGVLVDAVEG PAARAGFQKG DIILRIGDTD ITSAKQFEAV
AQNADPSKMV AVLVRRGDNT QFVPLRPRAP VQK
//
