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Database: UniProt
Entry: A0A0W0Z2J0_LEGSP
LinkDB: A0A0W0Z2J0_LEGSP
Original site: A0A0W0Z2J0_LEGSP 
ID   A0A0W0Z2J0_LEGSP        Unreviewed;       356 AA.
AC   A0A0W0Z2J0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=DegP protease (Do-like, S2-serine-like) {ECO:0000313|EMBL:KTD63352.1};
GN   Name=degP {ECO:0000313|EMBL:KTD63352.1};
GN   ORFNames=Lspi_1678 {ECO:0000313|EMBL:KTD63352.1};
OS   Legionella spiritensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=452 {ECO:0000313|EMBL:KTD63352.1, ECO:0000313|Proteomes:UP000054877};
RN   [1] {ECO:0000313|EMBL:KTD63352.1, ECO:0000313|Proteomes:UP000054877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mt.St.Helens-9 {ECO:0000313|EMBL:KTD63352.1,
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   -!- 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:KTD63352.1}.
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DR   EMBL; LNYX01000019; KTD63352.1; -; Genomic_DNA.
DR   RefSeq; WP_058483607.1; NZ_LT906457.1.
DR   AlphaFoldDB; A0A0W0Z2J0; -.
DR   STRING; 452.Lspi_1678; -.
DR   PATRIC; fig|452.5.peg.1843; -.
DR   OrthoDB; 9758917at2; -.
DR   Proteomes; UP000054877; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00987; PDZ_serine_protease; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KTD63352.1};
KW   Protease {ECO:0000313|EMBL:KTD63352.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054877};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..356
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006918205"
FT   DOMAIN          262..341
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   356 AA;  38452 MW;  301AEF17CCEE3FAD CRC64;
     MINKFSRFFL FVICVFSVVS LYASEQDDML ASEKNTIDIF QKFSPKVVFV HRLSEVANHS
     YEKMHVTTGA GSGIIWDAQG HIVTNFHVIK DADKLMITID NKTVPARVIG AEPRKDIAVL
     QIASPKALQS LKSFTPFTMA STNNLQVGQK VIAIGNPFGL DHSLTVGVIS ALGRQVPGIG
     GVTIRDMIQT DASINPGNSG GPLLDSKGRL LGMNTVIYSN SGASAGVGFA VPSDDIQRIV
     PQLIKNGRVI LSGLGIHRVE PGIASRLGVR KGILIAEVLP NTPAAGIGLR GTHRDGWGRI
     QLGDVIVALN GHPVRNYDDL YNLLTDIKVG ERVTLTVNRH NKMINYKIKT IDIAAY
//
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