ID A0A378JHP2_9GAMM Unreviewed; 457 AA.
AC A0A378JHP2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Carboxy-terminal protease {ECO:0000313|EMBL:STX50537.1};
DE EC=3.4.21.102 {ECO:0000313|EMBL:STX50537.1};
GN Name=ctpB {ECO:0000313|EMBL:STX50537.1};
GN ORFNames=NCTC13316_00619 {ECO:0000313|EMBL:STX50537.1};
OS Legionella busanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=190655 {ECO:0000313|EMBL:STX50537.1, ECO:0000313|Proteomes:UP000254794};
RN [1] {ECO:0000313|EMBL:STX50537.1, ECO:0000313|Proteomes:UP000254794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13316 {ECO:0000313|EMBL:STX50537.1,
RC ECO:0000313|Proteomes:UP000254794};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S41A family.
CC {ECO:0000256|ARBA:ARBA00009179, ECO:0000256|RuleBase:RU004404}.
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DR EMBL; UGOD01000001; STX50537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378JHP2; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000254794; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:STX50537.1};
KW Protease {ECO:0000256|RuleBase:RU004404, ECO:0000313|EMBL:STX50537.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..457
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016895245"
FT DOMAIN 95..163
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 457 AA; 49486 MW; A2F2E01FE3E724F6 CRC64;
MLTNQWYSGI LAALLTSTSL LPLPLMAAEE ATSNTEQTTP TRIPMEDVQR FSNAISEIKK
YYVKPVDDKQ LFDNAIRGML TGLDPHSDYL DEDEFKDLQT STAGEFGGLG IEVTMEDGVI
KVVTPLVDTP AFRAGIKAGD YIIKLGNRSV QGISLKDAVE LMRGKEGSTI DLTILRKGET
KPLVFSLVRE KIVIKSVKSK LLDGKYGYIR LTQFQAMTGQ DMEKAIAQLK QEAGGKLKGL
ILDLRNNPGG LLDSAIQIAD DFIDTNKKGD EELIVYTQGR LPGSKFTALA NPGDILDNAP
MVVLINNGSA SASEIVAGAL KDNKRAIIVG TQSFGKGSVQ TVLPLDDKRA IKLTTALYYT
PSGTSIQAKG ITPDIIIEEL EVAKNADDKK SIFSGFSEAD LSGHLDNGSS NNTEEKQPST
PIVEANDSIK DDQALLHEDY QLYTALTILK GLAVARK
//
