ID A0A1I6FP71_9RHOB Unreviewed; 446 AA.
AC A0A1I6FP71;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carboxyl-terminal processing protease {ECO:0000313|EMBL:SFR31741.1};
GN ORFNames=SAMN04488005_0163 {ECO:0000313|EMBL:SFR31741.1};
OS Yoonia tamlensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=390270 {ECO:0000313|EMBL:SFR31741.1, ECO:0000313|Proteomes:UP000199478};
RN [1] {ECO:0000313|Proteomes:UP000199478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26879 {ECO:0000313|Proteomes:UP000199478};
RA Varghese N., Submissions S.;
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; FOYP01000001; SFR31741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6FP71; -.
DR STRING; 390270.SAMN04488005_0163; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000199478; 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:SFR31741.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199478};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011465105"
FT DOMAIN 88..156
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 368..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 446 AA; 47265 MW; 97B1090FF3BC438C CRC64;
MKKLVFAALG GAALGLVTTV QVAGPLVAQD AQSSSNVYEQ LDLFGDIFER IRADYVQDVD
DKELIEAAIN GMLTSLDPHS SYMSAEAAAD MQINTRGEFG GLGIEVTQED GWVKVVSPMD
GTPADAAGIL AGDFITAVDG DSVMGLTLDE AVDLMRGPVG AEIIITVVRE GEVEPFDVSI
IRDTIKMTAV RSRTEGKAVV LRITTFNEQT FPNLNEGIAE QIAEAGGIDN VDGFILDLRN
NPGGLLNQAI YVSDAFLDAG EIVSTRGRDP QDGERFNATA GDLAQGKPIV VLVNGGSASA
SEIVAGALQD HRRAIVVGTN SFGKGSVQTV IPLSSDGAMR LTTARYYTPS GRSIQALGIS
PDIIVEQPRR QPDAEEEDGA RTQRTEASLR GALDNDSLTE DEIRQIEEDR ARAEAAAQLR
EDDYQLAYAI DILKGLNALG PVAGGN
//
