(data stored in SCRATCH zone)

SWISSPROT: A0A0E1P108_YERPA

ID   A0A0E1P108_YERPA        Unreviewed;       686 AA.
AC   A0A0E1P108;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 17.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|PIRNR:PIRNR001084};
DE            Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084};
DE            EC=3.2.1.23 {ECO:0000256|PIRNR:PIRNR001084};
GN   OrderedLocusNames=YPA_0418 {ECO:0000313|EMBL:ABG12386.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12386.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12386.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12386.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose
CC         residues in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001084};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family.
CC       {ECO:0000256|PIRNR:PIRNR001084}.
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DR   EMBL; CP000308; ABG12386.1; -; Genomic_DNA.
DR   RefSeq; WP_002209897.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12386; ABG12386; YPA_0418.
DR   EnsemblBacteria; AJJ81223; AJJ81223; CH58_3265.
DR   KEGG; ypa:YPA_0418; -.
DR   PATRIC; fig|360102.15.peg.3430; -.
DR   KO; K12308; -.
DR   OMA; SRRHYCF; -.
DR   BioCyc; YPES360102:GHZU-439-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; PTHR36447; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0E1P108.
DR   SWISS-2DPAGE; A0A0E1P108.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR001084,
KW   ECO:0000313|EMBL:ABG12386.1};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR001084,
KW   ECO:0000313|EMBL:ABG12386.1}.
SQ   SEQUENCE   686 AA;  78165 MW;  CBDA4617C9775AB4 CRC64;
     MSKFPPLSAK VSALLHGADY NPEQWENYPD IIDKDIAMMK QAKCNVMSVG IFSWVKLEPS
     EGEYNFSWLD ELIEKLYAAG IHIFLATPSG ARPAWMSQKY PEVLRVGRDR VPALHGGRHN
     HCMTSPVYRQ KVRQINQKLA ERYAHHPAVI GWHISNEYGG ECHCHSCQQK FRLWLQDRYQ
     TLDNLNEAWW SAFWSHTYSD WSQIESPAPQ GEVSIHGLNL DWRRFNTAQV TEFCSEEAKP
     LKAANPELPV TTNFMEYFYD YDYWKLAQVI DFISWDSYPM WHREKDETQL ACYTAMYHDL
     MRTLKQGRPF VLMESTPSAT NWQPTSKLKK PGMHILSSLQ AVAHGADAVQ YFQWRKSRGS
     VEKFHGAVVD HVGHIDTRVG REVSELGRIL EAMSPVMGSK VDADVAIIFD WESRWAMDDA
     EGPRNCGLEY EKTVAEHYRP FWERGIAVDI INADCDLSGY KLVIAPMLYM VREGFAERAT
     RFVEQGGQFV ATYWSGIVNE SDLCHLGGFP GPLRPLLGIW SEEIDCLADG ESNQVQGLAG
     NKAGLQGPYQ AIHLCDLIHL EGATAVARYR DDFYADRAAV TVNFVGEGKA WYVASRNDAA
     FQRDFFMNIA EELNLARALD TQFPYGVTAH RRTDGESEFI VVENYSNDSK SLVLPAVYRD
     MVDQQPVQGS LTLAPWGSRV LTRYLE
//

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