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Database: UniProt
Entry: Q5WXH7_LEGPL
LinkDB: Q5WXH7_LEGPL
Original site: Q5WXH7_LEGPL 
ID   Q5WXH7_LEGPL            Unreviewed;       782 AA.
AC   Q5WXH7;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   OrderedLocusNames=lpl1121 {ECO:0000313|EMBL:CAH15360.1};
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH15360.1, ECO:0000313|Proteomes:UP000002517};
RN   [1] {ECO:0000313|EMBL:CAH15360.1, ECO:0000313|Proteomes:UP000002517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens {ECO:0000313|EMBL:CAH15360.1,
RC   ECO:0000313|Proteomes:UP000002517};
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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DR   EMBL; CR628337; CAH15360.1; -; Genomic_DNA.
DR   RefSeq; WP_011215221.1; NC_006369.1.
DR   AlphaFoldDB; Q5WXH7; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   KEGG; lpf:lpl1121; -.
DR   LegioList; lpl1121; -.
DR   HOGENOM; CLU_358176_0_0_6; -.
DR   Proteomes; UP000002517; Chromosome.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..782
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004263937"
FT   DOMAIN          444..782
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   782 AA;  82917 MW;  7F61AB4A558CAA15 CRC64;
     MRYLLLLPGL LIAIVTSVNA NTSLKPSIAQ PTACVNSLFT AMGNQHWKSI VLKLTNNCNQ
     AVDFQNSTVS FQTTAALNTS FWGDFSPLSY PDNALNISSQ PQSGGNYLAT LNLHFPSYPG
     ANSKLPVGSS ISIKYGAVTD SHIEGTANVY LSTTVESGSI QLINAAAKPT NVSQGYALVH
     VTMNGQSVSD VQLPWETSKT LSGFAAGNYA ISAETVTDSN GNLYLGQANP SMVNVIANQT
     TSSTINYARV QETGKIKIHV QNLPGELSSY NENPTVLLTQ SQSGNSRSQL AVWGNTITVA
     ELKEGSSYQF STPAIQYNDY NCWPTFTPSS LVASAANIPT TNLTYQCAQI VKDNVTINVS
     GAPSSLASLK IILTPNDGSQ TVEQTIDLAN GVGSSAISLT DGVIYTLSSE SVPGYTVQFS
     PQPLTATENA TVNITLSPVT AAKGRIIGYV PGWKTPPAAQ ELASAGYTHV MIAFGVFSTN
     TPGVIVPAFE TITKEYIQSL HQAGIKVILS LGGALTSIPN TTVDFHQVLV ASSSPEAFKQ
     TFINSLKELI SQYGFDGFDI DIEHGINASG SFSQPQGDIA VLASIINTMY SQNSSLLITL
     TPQVANIAAT SGFDQTWGNY ASLIMQTHQS LAWVGIQLYN TGCAFGVDQV CYGPTPTDTP
     DFSVAMATDL LENWPATVNG RPTGFQPYIS YLRPSQIVIG YPSPNASGGS DGSPVTPTTT
     IKRAIQCLKT AIAGNTSCGA YVPPRAYGNI GGVFNWEVTY DKNNQFKFAK ELKNCAINGV
     CE
//
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