ID C0MCG2_STRS7 Unreviewed; 1546 AA.
AC C0MCG2;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN OrderedLocusNames=SZO_05310 {ECO:0000313|EMBL:CAW98510.1};
OS Streptococcus equi subsp. zooepidemicus (strain H70).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553483 {ECO:0000313|Proteomes:UP000001368};
RN [1] {ECO:0000313|EMBL:CAW98510.1, ECO:0000313|Proteomes:UP000001368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H70 {ECO:0000313|EMBL:CAW98510.1,
RC ECO:0000313|Proteomes:UP000001368};
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 33 family.
CC {ECO:0000256|ARBA:ARBA00009348}.
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DR EMBL; FM204884; CAW98510.1; -; Genomic_DNA.
DR KEGG; seq:SZO_05310; -.
DR PATRIC; fig|40041.11.peg.562; -.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG4409; Bacteria.
DR HOGENOM; CLU_246588_0_0_9; -.
DR Proteomes; UP000001368; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd08023; GH16_laminarinase_like; 1.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR011040; Sialidase.
DR InterPro; IPR026856; Sialidase_fam.
DR InterPro; IPR036278; Sialidase_sf.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR023364; Trans_sialidase_dom3.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR NCBIfam; TIGR01168; YSIRK_signal; 1.
DR PANTHER; PTHR10628; SIALIDASE; 1.
DR PANTHER; PTHR10628:SF25; SIALIDASE-1; 1.
DR Pfam; PF13088; BNR_2; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
DR PROSITE; PS51762; GH16_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:CAW98510.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 260..550
FT /note="GH16"
FT /evidence="ECO:0000259|PROSITE:PS51762"
FT REGION 1242..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1546 AA; 169787 MW; EC1A64DB75AB7E72 CRC64;
MLFNPIGKEQ IRKYAIKKLS VGVASVCVGI GLAAGLPVVV YADDVSEVSL QQPTKAAVTE
ISHEQEPQAT DTDSEALVVS EETTVDEAVV ANAVTSNAAD QTADEEKSNA PVELNKVANG
GFDNDYVSNK NQWQYREGGH SVLTTENNNS YAEVTSGTLD EHILQKVSTT VGKTYTLEAD
VKVEADTPHN GLYLTAKESN HNLQGPVIKE VSLTDTDGTW SHIKLSFTAT TSETFVGLVK
RLEASSPETL AASASIDNVS VVEENDYELI WQDEFSGDQL NQENWGYELG SIRGNEQQHY
TDSTENIYLE NGNLVLNVTE RKGEDRYANP RGGTSARQVI YDSGSVRTVG KQEFLYGRIE
ARAKLPKGKG AFPAFWTLGA DFTLDGDIAS TQGYGWPSTG ELDIMELIGA PNGEHEGELA
EGDQSNKTVY GTPHFYYVKG DADKDGSYSP TALGGNLTLS DDFYDDYHIF GINWYPDKIE
WYVDGIVYNT MYLTGDERLE AAAAAFNKPQ YLQFNLATGG NWSKNAGYYL ASDETAFVID
YVRYYQDAEQ KAASEAYYAS QPDLKGVKDL TMLEGTSPDL AQAVTTDQEG YVVDFSVENE
YLFTNKGGNT NAALQAAGRD DLSALSELAP GIYNIYYSAV PYNADLGSTV TPTAKIAREV
AILTVLPKEG LIGKKGEPLS TVALPANWQW VTPEEILGSA EHYQIKYTTE GGRAIYTSIE
ASYISDQPIS DQASILVDLG NAILDATAEK AAVTDDEALS KLDDVMSLNQ GTVTIRYRLD
TADTTVRSSS PLALLSISNQ ASANEYASFF IEPKNNKIGL EFKGAEVPIV KVGSGFNLLT
NSDWQTISYV FTGSRLKIYL NGDLYGEADF AGFMKQLPWK ASADTLTIGG LKRTYDGESV
LHWGLKGLVD QVLIDTDVYD LTDIAKAHQS TLRPVTGEKT NVWDKYDEGV FEYRIPSVVK
TPSGTLIAAA DARKKHYNDW GDVATVVRIS HDDGKTWSNN ITVLDMPTQP YFTTQYSLAD
WNTNMTQSAF SIDSTLLTDA SGKLYLLVDV FPESQGAVAS KAGSGYELIN GQYYLNLYDF
DNNKYTVREG GIVYDQNGHQ TDMYVDEGNF ETAFSTRGNL YQTEAGEDIL LGNIYLRSGR
TKQGITREGS QTAPLFTYMT SFLWLLTSED EGQTWSTPLD ITPQIKEDWM GFLGTGAAAG
IEIDAVNAEG EQVKRLVFPI YYTNQQNATS ASLGRQSSAN IFSDDGGQTW QRGESPNDGR
IYGHNQQTTS KDFDTSVTEL TENQIIQLNN GHLLQFMRNT GKTIVIARST DYGATWEDNP
TVTDLPEPYV NLSAIHMMVD GKEYVVLSNP LGEPSGEQLT IRNQRMKGIL RVGEVLEDDS
INWVASTIFE PKRFAYSSLV QLDDERVGLL YEYSGQITYS TFNIKQMISD QFREDKAEIE
EVTITSAAPK QNGKASITIQ MTFNQPMFIL GDRQLAVTVN GVDKLASYVS GDGTDTAIFE
LSLESMPEGP ITVLPQFDHT IVETKYGIRL TDDKAYTVSY PAAVTA
//
