ID A0A1H0ZDB7_9BURK Unreviewed; 524 AA.
AC A0A1H0ZDB7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SDQ25417.1};
GN ORFNames=SAMN05443245_0586 {ECO:0000313|EMBL:SDQ25417.1};
OS Paraburkholderia fungorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=134537 {ECO:0000313|EMBL:SDQ25417.1, ECO:0000313|Proteomes:UP000183487};
RN [1] {ECO:0000313|Proteomes:UP000183487}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS106B {ECO:0000313|Proteomes:UP000183487};
RA Varghese N.;
RL Submitted (OCT-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 ---------------------------------------------------------------------------
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; FNKP01000001; SDQ25417.1; -; Genomic_DNA.
DR RefSeq; WP_074762878.1; NZ_FNKP01000001.1.
DR AlphaFoldDB; A0A1H0ZDB7; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000183487; 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, ECO:0000313|EMBL:SDQ25417.1};
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..524
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010197955"
FT DOMAIN 91..159
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 404..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 57034 MW; DC7CB0D31EBB15CC CRC64;
MRKNLKNIGL IAVGLATGAF ATLQLSASAQ QPASATAPLP LDQLRLFAEV FGQIKHEYVE
PVDDKKLLTA AIKGMVSSLD PHSSYLDKTD YEELQEQTKG RFAGLGIEIS SEDGLIKVIS
PIEDTPAFRA GIRPGDLITR INDKPVRGMT LDQAVKQMRG DPGTKVTLTI FRKTDDRTFP
LTVTRAIIKV QSVKGKVLAP GYAYVRITSF QERTVPDLAA KLQDIARQSP NLKGLILDLR
NNGGGLLQSA VGVAGAFLPP NSVVVSTNGQ IPDSKQVYRD TYDNYRLQSF DSDPLKDVPA
IFKTVPMVVL TNAYSASASE IVAGALQDQR RALIVGKTTF GKGSVQTVRP MTADTALRLT
TAYYYTPSGR SIQNKGIRPD VAVDQYADGD PDDALVTREV DYSNHLANTQ DPNEKKEAEQ
REQDRMDQLR LLEEANDKKT PEQRQKDRDR KPVEFGSADD FMMQQGLNKL EGKPVQESKS
LSERRLAQNK PETSASAPVA VKPTQPVPGA SGTAPASAPA TQGK
//
