ID A0A0W0X2T0_9GAMM Unreviewed; 441 AA.
AC A0A0W0X2T0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carboxy-terminal protease {ECO:0000313|EMBL:KTD38892.1};
GN Name=ctpA {ECO:0000313|EMBL:KTD38892.1};
GN ORFNames=Lnau_0386 {ECO:0000313|EMBL:KTD38892.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD38892.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD38892.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD38892.1,
RC ECO:0000313|Proteomes:UP000054725};
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:KTD38892.1}.
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DR EMBL; LNYO01000004; KTD38892.1; -; Genomic_DNA.
DR RefSeq; WP_058503466.1; NZ_LNYO01000004.1.
DR AlphaFoldDB; A0A0W0X2T0; -.
DR STRING; 45070.Lnau_0386; -.
DR PATRIC; fig|45070.6.peg.408; -.
DR OrthoDB; 9812068at2; -.
DR Proteomes; UP000054725; 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:KTD38892.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU004404}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..441
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006916085"
FT DOMAIN 89..157
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 441 AA; 47556 MW; C46C34AF56ABFF40 CRC64;
MHKRRFYFGA MVTVVTTALI FPAQAFPAED QSGTKQIPME DVQRFSNAIG EIKKYYVKPV
DDKELFDNAI RGMLSGLDPH STYLDEDSFK ELQTSTSGEF GGLGIEVTME DGVVKVVTPL
VDTPAFKAGI KSGDYIIKLG SKSVQGISLK EAVELMRGKE GTTLDLTILR KGENKPLTFS
LVREKILIKS VKSKLLDDGY GYIRLTQFQA MTGQDMEKAI AQLKQQSGGN LKGLILDLRN
NPGGLLDSAI QVSDAFLATG KDGKPEMIVY TQGRLPGSKF TALTTNSKDI LNNAPMVVLI
NNGSASASEI VAGALKDNKR AVILGTKSFG KGSVQTVLPL DDKRGIKLTT ALYYTPSGTS
IQAKGITPDI VVEELEVPKT APKTDAFAGF SEADLSGHLL NKSEGQATNG NAIKDDDALL
HEDYQLYAAL TILKGLSVAH R
//
