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Database: UniProt
Entry: Q8ZRK1_SALTY
LinkDB: Q8ZRK1_SALTY
Original site: Q8ZRK1_SALTY 
ID   Q8ZRK1_SALTY            Unreviewed;       273 AA.
AC   Q8ZRK1;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 98.
DE   SubName: Full=Xylanase/chitin deacetylase {ECO:0000313|EMBL:AAL19260.1};
GN   Name=ybeJ {ECO:0000313|EMBL:AAL19260.1};
GN   OrderedLocusNames=STM0303 {ECO:0000313|EMBL:AAL19260.1};
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL19260.1, ECO:0000313|Proteomes:UP000001014};
RN   [1] {ECO:0000313|EMBL:AAL19260.1, ECO:0000313|Proteomes:UP000001014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720
RC   {ECO:0000313|Proteomes:UP000001014};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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DR   EMBL; AE006468; AAL19260.1; -; Genomic_DNA.
DR   RefSeq; NP_459301.1; NC_003197.2.
DR   RefSeq; WP_000119390.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRK1; -.
DR   STRING; 99287.STM0303; -.
DR   PaxDb; 99287-STM0303; -.
DR   GeneID; 1251822; -.
DR   KEGG; stm:STM0303; -.
DR   PATRIC; fig|99287.12.peg.320; -.
DR   HOGENOM; CLU_030024_3_1_6; -.
DR   OMA; HTNDLHY; -.
DR   PhylomeDB; Q8ZRK1; -.
DR   BioCyc; SENT99287:STM0303-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10969; CE4_Ecf1_like_5s; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR34216; -; 1.
DR   PANTHER; PTHR34216:SF7; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE N-DEACETYLASE; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000313|EMBL:AAL19260.1};
KW   Glycosidase {ECO:0000313|EMBL:AAL19260.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AAL19260.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:AAL19260.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Xylan degradation {ECO:0000313|EMBL:AAL19260.1}.
FT   DOMAIN          61..273
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
SQ   SEQUENCE   273 AA;  31922 MW;  CDEEFC0C65C4BC26 CRC64;
     MSYARHLPVL MYHHVSDKPG QITLSPRTFR AQMKWLAESG WKTVTAAEVE AFYHGARLPR
     KSVMLTFDGG WLDNWLQVFP VLQEFNLHAH LFLVTSLISD GPVRIPAGEP VYSHDECQML
     VKQGRADEVM LRWSEVREMH LSGLVEFHSH THTHRRWDQK PVSRNPSDLL RVDILLSRKR
     MREMLGYCSQ HLCWPEGWYC SDYIHVAEEL GFTYLYTTER RMNNPVIGSQ RIGRINAKER
     KNVGWLKRRL FYHTTPGFSS LLARHKGARR IAD
//
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