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Database: UniProt
Entry: G5QV01_SALSE
LinkDB: G5QV01_SALSE
Original site: G5QV01_SALSE 
ID   G5QV01_SALSE            Unreviewed;       587 AA.
AC   G5QV01;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Chitinase {ECO:0000313|EMBL:EHC94440.1};
GN   ORFNames=LTSESEN_0439 {ECO:0000313|EMBL:EHC94440.1};
OS   Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC94440.1, ECO:0000313|Proteomes:UP000005065};
RN   [1] {ECO:0000313|EMBL:EHC94440.1, ECO:0000313|Proteomes:UP000005065}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-543 {ECO:0000313|EMBL:EHC94440.1,
RC   ECO:0000313|Proteomes:UP000005065};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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:EHC94440.1}.
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DR   EMBL; AFCU01000145; EHC94440.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5QV01; -.
DR   SMR; G5QV01; -.
DR   PATRIC; fig|913082.3.peg.349; -.
DR   BioCyc; SENT913082:G120J-2259-MONOMER; -.
DR   Proteomes; UP000005065; Unassembled WGS sequence.
DR   GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR   CDD; cd00325; chitinase_GH19; 1.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR22595:SF208; CHITINASE; 1.
DR   PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..587
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003482970"
FT   DOMAIN          431..519
FT                   /note="PKD/Chitinase"
FT                   /evidence="ECO:0000259|SMART:SM00089"
SQ   SEQUENCE   587 AA;  63681 MW;  C488AD17A6644D60 CRC64;
     MGLQKTLALS AVAAGIMLSL SGAQAAPLLS SSEPMTINAS DLAAKEKALT DFPLMEAVKS
     SIQTLDNSAV EQIEPGRAAN PANVKRVESI LKEADWDYLF PMRAPEYTYS NFLKAIGKFP
     AVCGTYTDGR DSDAICRKTL ATMFAHFAQE TGGHESWRDI PEWRQALVYL REVGWTEGQK
     GGYNGECNPD VWQGQTWPCG KDKDGDFLSY FGRGAKQLSY NYNYGPFSDA MYGDVRPLLD
     KPELVADTWM NLASAVFFFV YPQPPKPSML HVIDGTWQPN DRDKANGLVS GFGVTIQIIN
     GGVECGGADE NAQSLNRIAY YKEFANYLKV PVPADEVLGC KKMKQFDEGG AGALPIYWEQ
     DWGWSADTAD GKTYSCQLVG YQTPYTAFKE GDYTKCVQHY FNVNVVDDNG TTEPDVTPTP
     APVTDENVAP VARIAGPVGA VEAGSPVSLS AEGSTDANGD KLTYTWMSQD GKTLSGQDKA
     VVIFNAPDVT QNTQYVVNLT VSDGTLSSTA VYTLNVKAKA AAADDEDKTT SYPAWSSSQK
     WNPGDIVNSN GALYQCKPFP EGSWCNVAPA YYEPGVGIAW ADAWNAL
//
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