ID A0A1Q8J3I5_9BURK Unreviewed; 525 AA.
AC A0A1Q8J3I5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidase S41 {ECO:0000313|EMBL:OLL33460.1};
GN ORFNames=BTH42_01765 {ECO:0000313|EMBL:OLL33460.1};
OS Burkholderia sp. SRS-W-2-2016.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1926878 {ECO:0000313|EMBL:OLL33460.1, ECO:0000313|Proteomes:UP000186182};
RN [1] {ECO:0000313|Proteomes:UP000186182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRS-W-2-2016 {ECO:0000313|Proteomes:UP000186182};
RA Chauhan A.;
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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:OLL33460.1}.
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DR EMBL; MSDV01000005; OLL33460.1; -; Genomic_DNA.
DR RefSeq; WP_075295155.1; NZ_MSDV01000005.1.
DR AlphaFoldDB; A0A1Q8J3I5; -.
DR STRING; 1926878.BTH42_01765; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000186182; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07560; Peptidase_S41_CPP; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR004447; Peptidase_S41A.
DR InterPro; IPR005151; Tail-specific_protease.
DR NCBIfam; TIGR00225; prc; 1.
DR PANTHER; PTHR32060:SF22; CARBOXYL-TERMINAL-PROCESSING PEPTIDASE 2, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR32060; TAIL-SPECIFIC PROTEASE; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF03572; Peptidase_S41; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU004404};
KW Protease {ECO:0000256|RuleBase:RU004404};
KW Reference proteome {ECO:0000313|Proteomes:UP000186182};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..525
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012728651"
FT DOMAIN 92..160
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 370..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..525
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 57263 MW; E2692C88A6E61EAF CRC64;
MRKNLKNIGL IAAGLATGVF ATLQFSASAE QPASAVVAPL PLDQLRLFAE VFGQIKHEYV
EPVDDKKLLT SAIKGMVSSL DPHSSYLDKT DYEELQEQTK GRFAGLGIEI SSEDGLIKVI
SPIEDTPAFR AGIRPGDLIT RINDKPVRGM TLDQAVKQMR GEPGTKVTLT IFRKTDDRTF
PLTVTRAVIK VQSVKGKIVA PGFAYVRITS FQERTTPDLA AKLQDLARQE PNLKGVILDL
RNNGGGLLQS AVGVAGAFLP PNSVVVSTNG QIPDSKQIYR DTYDNYRLQS FDSDPLKDVP
AIFKTVPMIV LTNAYSASAS EIVAGALQDQ HRALILGKTT FGKGSVQTVR PMTADTALRL
TTAYYYTPSG RSIQNKGIRP DLPVDQYADG DPDDALVTRE VDYSNHLANT QDPNEKKEAE
QREQERMEQL RQLEEQNDKK TPEQRQKDRE RKPVEFGSAD DFMLQQALNK LEGKAVQQSK
SIMERRLAQN KPATSASAPV AVKPTQPVPG ASGPAPASAP APAGK
//