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}.
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; 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
//