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Database: UniProt/TrEMBL
Entry: F5WSV3_ERYRF
LinkDB: F5WSV3_ERYRF
Original site: F5WSV3_ERYRF 
ID   F5WSV3_ERYRF            Unreviewed;      2091 AA.
AC   F5WSV3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   22-NOV-2017, entry version 39.
DE   SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:BAK31835.1};
GN   OrderedLocusNames=ERH_0780 {ECO:0000313|EMBL:BAK31835.1};
OS   Erysipelothrix rhusiopathiae (strain Fujisawa).
OC   Bacteria; Firmicutes; Erysipelotrichia; Erysipelotrichales;
OC   Erysipelotrichaceae; Erysipelothrix.
OX   NCBI_TaxID=650150 {ECO:0000313|EMBL:BAK31835.1, ECO:0000313|Proteomes:UP000007944};
RN   [1] {ECO:0000313|EMBL:BAK31835.1, ECO:0000313|Proteomes:UP000007944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fujisawa {ECO:0000313|EMBL:BAK31835.1,
RC   ECO:0000313|Proteomes:UP000007944};
RX   PubMed=21478354; DOI=10.1128/JB.01500-10;
RA   Ogawa Y., Ooka T., Shi F., Ogura Y., Nakayama K., Hayashi T.,
RA   Shimoji Y.;
RT   "The genome of Erysipelothrix rhusiopathiae, the causative agent of
RT   swine erysipelas, reveals new insights into the evolution of
RT   firmicutes and the organism's intracellular adaptations.";
RL   J. Bacteriol. 193:2959-2971(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|SAAS:SAAS00568376}.
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DR   EMBL; AP012027; BAK31835.1; -; Genomic_DNA.
DR   RefSeq; WP_013852917.1; NC_015601.1.
DR   ProteinModelPortal; F5WSV3; -.
DR   STRING; 650150.ERH_0780; -.
DR   EnsemblBacteria; BAK31835; BAK31835; ERH_0780.
DR   KEGG; erh:ERH_0780; -.
DR   eggNOG; ENOG4105CNT; Bacteria.
DR   eggNOG; COG3250; LUCA.
DR   KO; K01190; -.
DR   OMA; MQYRTLA; -.
DR   OrthoDB; POG091H0F66; -.
DR   BioCyc; ERHU650150:GHGV-809-MONOMER; -.
DR   Proteomes; UP000007944; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; -; 3.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011081; Big_4.
DR   InterPro; IPR032311; DUF4982.
DR   InterPro; IPR000421; FA58C.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR006101; Glyco_hydro_2.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR006104; Glyco_hydro_2_N.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF07532; Big_4; 4.
DR   Pfam; PF16355; DUF4982; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   Pfam; PF02837; Glyco_hydro_2_N; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007944};
KW   Glycosidase {ECO:0000256|SAAS:SAAS00080608};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00080540};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007944};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     32       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        33   2091       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5003333853.
FT   DOMAIN     1034   1192       F5/8 type C. {ECO:0000259|PROSITE:
FT                                PS50022}.
SQ   SEQUENCE   2091 AA;  232623 MW;  621244E0B596C929 CRC64;
     MNSSFRKAVK IMGVVVAVTC SSVFIEKTPI HAAVVEPVVT KTDSRNVDFN DDWKFKLNVS
     GTSSPSEIDY DETDWQALSL PHDWSIFFDF DHNSPAQNEG GLLNGGTGWY RKTFVFDKKM
     DKNVRLNFGG VYMDSTVFVN GKEVGNYPNG YTPFSYDITS YLNQEGPNTI AVKVVNKQPS
     SRWYSGSGIY RDVSLTYTDD VSIKEYGTTV LTPNLDKEVG KDVTTEVKTT VLNKSKKAEK
     VKVKTEVVTV DGTSMGKAET KEVEIQAGKE QTLDSTIMVS NPSLWDIDSP VTYRVKTQVL
     KSNRVVDETV ERFGYRYMNW TPSGGFSLNG NDVKFYGVSM HHDQGALGSV ANYDAMRRQM
     EILKDMGVNS VRITHNPADD KLLAIAEDLG LMIIDEAFDT WYGGKKPYDY GRFFEAKATH
     PEALDGQSWA EYDLKRMVAR GKNSPAVIMW SLGNEIGESN SGSAKAVQTI RNLHRWTKEV
     DDTRYTTMGQ DVYRWAPTGG HELISAEVDA VGINYAEDSY KAIRAKHPDW LIYGSETSSA
     TRSRGVYAFP DELRSHDNSA ARKYQQSDYG NDHVGWGKTA TNSWIPDRDE KGYAGQFIWT
     GFDYIGEPTP WHNQNQTPPK SSYFGIIDTA GFPKNDFYLY QSQWKDVETD PMVHILPHWN
     WEKESLLDYN MRTRDGKIPV RIFSNAAKVE LFLDDVSLGE KAFVQKTTAY GRPYQEGANA
     KELYLEWRLD FKPGTLKAIA KDKDGNVIAE DVIKTSKGSA AVELVPEKRV IQNGRDHLSY
     IHVNVVDENG VMNPNAQNNI IFTLEGNGEI VGVDNGDPAS NERYKAQHDG TWQRKAFNGK
     ALVIVKSDGQ EGSFKLTAKA ENLSEGKTEV FAIEKKPETP SILGFDDVSV FTETHVQPEL
     PKTVNAIYSD GSEKAVDVNW ETIEASKLEQ PGSFSVKGTV EGVAIPVNAT VLVRMITDLI
     DPVLATPKGT MPSLPSTVIA YYSNGAEVNL PVTWESITDA MIAEAGVLKI SGQAHSGGQD
     YPVFAHITVL EATAVQENIA IRRPQDTYPI ATSSYMSGGD RIERINDGTI AFENRWTNWV
     NNFGDKQEEW VMLEFEKIET IHQVGIHFFT DNTTKVPASL TIETSVDGVT FTPVVNQSKN
     NNFVVTSGDV KTEIPIKFDK VDAKFVRLNM TSQMNGDKPR PMGLSELKVI GDTFKIEANS
     KAELEMIHLD TKPLENFKVD QNVYVVGVPF GKALPVLKGT AKAGSFVNVV QPTRDNNYQG
     KVRVTSEDGL NSKDYDVTYV VSDPVYDHTT LTLDRIEGKT QETIPFKTES LLEDGTAIAP
     SLLDITYEVV QGDASGIRMN AGLIYLHKEG TYTVKAHVSY GGKTYESNEV SFTVTKNEVQ
     EPIKAFKPVV IRTERSQKIE LPKTVTAQYE TLFDKDVAVT WDAFDVLRLD EYGTFEIKGR
     VEGTDIQAVA KVIVEGYVGV ESFSLVTPKD KSFKLPLKAK AYHNTGRVDE FNVVWEAFDK
     ENLKTPGTYI LKGMVETANT ETTLTIRVAA EYEKGDNIAK MWTGSELPAA IASFTNDGPG
     SNDRVSAMND AVISYTNTPA NRWTNWQAQS REKDWVGIVF ADAGTMAPRF VDNFNIGFFE
     DNGTGYPGSY VIEVLKEGIK PELPTKFGHI SSEDSVLNDP NNWVEVQNLK AKPFAYQTMN
     TLTFDGVETY AVRINMTKQA NKKGLAVTEI EVYDRIAKAH QDFTVTLKVD GKDVDAFTQD
     HNFVYEQKTN NLPSLELQAT NNANITAIEI ENGMKYVVRA EDGIKTETYT ITYDTSIRDA
     RNALVKMISK AKNVEIEGYE SLGVQAMQAS ILKAQTAVED LNTDVKTLQS LTKLLEKNID
     DLVAVGDQID KARESLQAMI DIAESIDRTL YTDESLAALD KQLSFAKVSY EDDSATTVIL
     DVVTQNLREA IFGLEYRDQT VKGPFDSITM NPKVSFEGST PITEEAFINA LNIQNPDGVA
     FDIETNFMEL VDQNTEGTYA VTVRLIRAQR AFFRMKSNPY VKEFKVDVTI QGESSKPIVT
     EPKEESVTPE APTTPPSTLP TTGVGTRNVS ILITLGGLMY VVSLKKKRKQ K
//
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