ID K4QYJ3_STRDJ Unreviewed; 371 AA.
AC K4QYJ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Endochitinase {ECO:0000313|EMBL:CCK25895.1};
GN ORFNames=BN159_1516 {ECO:0000313|EMBL:CCK25895.1};
OS Streptomyces davaonensis (strain DSM 101723 / JCM 4913 / KCC S-0913 / 768).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK25895.1, ECO:0000313|Proteomes:UP000008043};
RN [1] {ECO:0000313|EMBL:CCK25895.1, ECO:0000313|Proteomes:UP000008043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101723 / JCM 4913 / KCC S-0913 / 768
RC {ECO:0000313|Proteomes:UP000008043};
RX PubMed=23043000; DOI=10.1128/JB.01592-12;
RA Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R., Blom J.,
RA Pelzer S., Kalinowski J., Mack M.;
RT "Genome sequence of the bacterium Streptomyces davawensis JCM 4913 and
RT heterologous production of the unique antibiotic roseoflavin.";
RL J. Bacteriol. 194:6818-6827(2012).
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DR EMBL; HE971709; CCK25895.1; -; Genomic_DNA.
DR RefSeq; WP_015656290.1; NC_020504.1.
DR AlphaFoldDB; K4QYJ3; -.
DR STRING; 1214101.BN159_1516; -.
DR KEGG; sdv:BN159_1516; -.
DR PATRIC; fig|1214101.3.peg.1536; -.
DR eggNOG; COG3179; Bacteria.
DR HOGENOM; CLU_045506_0_0_11; -.
DR Proteomes; UP000008043; Chromosome.
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; cd00161; RICIN; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.80.10.50; -; 2.
DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR22595:SF208; CHITINASE; 1.
DR PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008043};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..371
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003879484"
FT DOMAIN 33..157
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 371 AA; 38873 MW; D90EFE399B892516 CRC64;
MSTPRLIGRG TVLAVLAALL AALFSATPAQ AASGTITGLA GKCVDVAGAS SANGTAVQLY
DCNGTGAQVW SNSGDGTLRA LGKCLDVVDR STADGASVQL WDCSGGANQQ WVVTSARDIV
NPAANKCLDV RDNTSANGTR LQIWSCTGGA NQKWSAPASG GGTTPSGFVV SEAQFNQMFP
NRNSFYTYSG LRAALSAYPG FANTGSDTVK KQEAAAFLAN VNHETGGLVH VVEQNTANYP
HYCDWGQPYG CPAGQAAYYG RGPIQLSWNF NYKAAGDALG LDLLNNPWLV QNDASVAWRT
GLWYWNTQTG PGTMTPHNAM VNQAGFGQTI RSINGSLECD GKNPAQVQSR VDAYNRFTSI
LGVSPGGNLY C
//
