ID C0MC32_STRE4 Unreviewed; 1147 AA.
AC C0MC32;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Glycosyl hydrolase family 2 protein {ECO:0000313|EMBL:CAW94727.1};
GN OrderedLocusNames=SEQ_1682 {ECO:0000313|EMBL:CAW94727.1};
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482 {ECO:0000313|EMBL:CAW94727.1, ECO:0000313|Proteomes:UP000001365};
RN [1] {ECO:0000313|EMBL:CAW94727.1, ECO:0000313|Proteomes:UP000001365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047 {ECO:0000313|EMBL:CAW94727.1,
RC ECO:0000313|Proteomes:UP000001365};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; FM204883; CAW94727.1; -; Genomic_DNA.
DR RefSeq; WP_012679921.1; NC_012471.1.
DR AlphaFoldDB; C0MC32; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR KEGG; seu:SEQ_1682; -.
DR HOGENOM; CLU_006501_0_1_9; -.
DR OrthoDB; 9762066at2; -.
DR Proteomes; UP000001365; Chromosome.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
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 PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 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; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAW94727.1}.
FT DOMAIN 35..178
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 216..298
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 308..491
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 671..753
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 788..872
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
SQ SEQUENCE 1147 AA; 128813 MW; 343239106B2E3CCC CRC64;
MSVETITGST DQSHGDIYQL HWIDKVGRCH AFSKGWRFLM ADLQLAQEPF FDDSDWQQIA
LPHDFSINQP YTVNGEAQSA YKLGGVGWYR KYFALDPKLA DHKVYVTFDG AYMETQVYLN
GHLIGEHVNG YQAFSYDLSA FVIPGQENLL AVRVEHLVPS SRWYSGSGLY REAFLTVLPK
VHLDKDRLRL SLSQAALEAD SQALEIELGL SQQVPLSGYQ LSLSLFEQLA DIQQRQTVYE
SKPVALDLLE ESGRLVMTIP LRHIKLWSPA QPQLYQLDML LYHKGAVLDR LTLETGFRQL
HFDAECGFFL NGKAFKLQGV CLHHDQGSLG ACAYEEAIAR QLVLLKEMGA NTVRVTHNPS
ARRLKDLANR LGLFLIEEAF DTWTYAKNGN SHDFSSHFHK TVGHQNAARL KGVTTAETTW
AQYSIQAMVL SGLHDPSVLM WSIGNELLEG FSADVSHYPY VAKELCQWIT ELDQSRPITL
GDNKLKDKHF HWAQETKALA EQVNQLQSVQ GVIGLNYAKA RDYDRLHRDN PTWLLYGSET
ASAINSRGVY HLKGGASQDH ELTSYDQSTV DWGSLASEAW YDTITRDFVA GECVWTGFDY
LGEPTPWNKI DSGAADQWPS PKQSYFGILD TAGFAKDSYY FYQSQWSKDK TTLHILPSWQ
EKDLQLDDQG MVEVVVYSNA ASVRILFDDG HGGQIDYGIK TLTRHETPAG HCYQLYEGDD
AAELPHQNLY LTWKLPYRSG SLRAIAYDDK GQVLTQTSGR SCVSSYQQPA QLSWSCFEPP
KLLAEPALLY LELSLLDANE TLVLSANPVI KLEVEGPGAC LALDNGDPRD HRPYTALSRR
AYGGKLLAII ALDGRAGQLR ITARAAGFVE ASYQLTVSEA AVNEKLLAYQ LDKYSFITNE
TNKPSKPYAR SRGSAVDSLM PNPDSCLKRQ GHYLPDNSVM VFSYTTALSR PLTFQPLIKR
LLKGNDIILP DWLQPRAAAG QLFTKAFPID WQLTEAVFSE ESRVSGQTLC FGEALELEAI
LKSDTKGLRI NQELSLVAKK KRLFQSDTQL SYRYQYDTIQ AIGAISLTGL KKPLSSLRLV
LDYRSSTNAP SKQLILSLDQ IEQPCHYIML EEVVDVLSLD LTLEQPIRQA FDLARLQLGL
WSMVEEA
//
