ID A0A0W0Z9S8_LEGSP Unreviewed; 441 AA.
AC A0A0W0Z9S8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carboxy-terminal protease {ECO:0000313|EMBL:KTD65885.1};
GN Name=ctpA_1 {ECO:0000313|EMBL:KTD65885.1};
GN ORFNames=Lspi_0304 {ECO:0000313|EMBL:KTD65885.1};
OS Legionella spiritensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=452 {ECO:0000313|EMBL:KTD65885.1, ECO:0000313|Proteomes:UP000054877};
RN [1] {ECO:0000313|EMBL:KTD65885.1, ECO:0000313|Proteomes:UP000054877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD65885.1,
RC ECO:0000313|Proteomes:UP000054877};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD65885.1}.
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; LNYX01000004; KTD65885.1; -; Genomic_DNA.
DR RefSeq; WP_058482252.1; NZ_LT906457.1.
DR AlphaFoldDB; A0A0W0Z9S8; -.
DR STRING; 452.Lspi_0304; -.
DR PATRIC; fig|452.5.peg.337; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000054877; 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:KTD65885.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054877};
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..441
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006918411"
FT DOMAIN 87..155
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 441 AA; 48142 MW; D1C6350C06B880B4 CRC64;
MFRKQLFSSV LIVLFTTAYM IPPQVVAAEE TTSRIPMEDV QRFSNAISEI KKYYVKPIED
KELFDNAIRG MLSGLDPHST YLDENAFKEL QTSTSGEFGG LGIEVTMEEG VVKVVTPLVD
TPAFKAGIKA GDYIIKLGPK SVQGLSLQNA VHLMRGKEGT TINLTILRKG VNKPLEFSLI
REKIVIKSVK SKLLDNNYGY VRLTQFQAMT AKDMRKAIEQ LKQQAGGKLN GLILDLRNNP
GGLLDSAIQV ADSFINNDKK GNEEMIVYTQ GRLPGSKFTA LANPGDILHN APLVVLINNG
SASASEIVAG ALKDNKRAII IGTRSFGKGS VQTVLPLDEK RGIKLTTALY YTPAGISIQA
KGIIPDIVVE EMEIPKNAKA KAGFDFSEAE LNGHLLNKSE GEDAAKQSEE ISSKNDNTLL
HEDYQLYTAL TILKGLAIAK R
//
