ID A0A2S4MNK6_9BURK Unreviewed; 523 AA.
AC A0A2S4MNK6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:POR56281.1};
GN ORFNames=B0G62_101679 {ECO:0000313|EMBL:POR56281.1};
OS Paraburkholderia eburnea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1189126 {ECO:0000313|EMBL:POR56281.1, ECO:0000313|Proteomes:UP000237381};
RN [1] {ECO:0000313|EMBL:POR56281.1, ECO:0000313|Proteomes:UP000237381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18070 {ECO:0000313|EMBL:POR56281.1,
RC ECO:0000313|Proteomes:UP000237381};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JAN-2018) 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:POR56281.1}.
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DR EMBL; PQGA01000001; POR56281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4MNK6; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000237381; 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:POR56281.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000237381};
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..523
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015758372"
FT DOMAIN 92..160
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 432..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 57165 MW; BB906B6183AD154D CRC64;
MRKNLKNIGL IAAGLATGVF ATLQISASAQ QTQQTVIEPL PLDQLRLFAE VFGQIKHEYV
TPVDDKKLLT AAIKGMVSSL DPHSSYLDKT DYQELQEQTK GRFAGLGIEI SSEDGLIKVI
SPIEDTPAFR AGIRPGDLIT RINDKPVRGM TLDQAVKQMR GDPGTKVTLT IFRKTDDRTF
PLTITRAIIK VQSVKSKILA PGYAYIRITS FQERTTPDLA AKLQDIARQE PNLKGLILDL
RNNGGGLLQS AVGVAGAFLP ADSVVVSTNG QIPDSKQVYR DNYENYRLPS FDGDPLKGEA
AEFKTVPMIV LTNAYSASAS EIVAGALQDQ KRALIIGKTT FGKGSVQTVR PMTADTALRL
TTAYYYTPSG RSIQNKGIRP DVAVDQYADG DPDDALVTRE VDYSNHLANT QDPDEKKEQD
LREQERMDML RQLEEQNDKK TPEQRQKDRD RKPVEFGSND DFMLQQALNK LQGKPVTESK
SPMERRLAQA KPPTSASAPI AVKPSASAVP GASTPAPASA PAK
//
