ID   B2IRU8_STRPS            Unreviewed;       980 AA.
AC   B2IRU8;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=exo-alpha-sialidase {ECO:0000256|ARBA:ARBA00012733};
DE            EC=3.2.1.18 {ECO:0000256|ARBA:ARBA00012733};
GN   Name=nanA {ECO:0000313|EMBL:ACB90917.1};
GN   OrderedLocusNames=SPCG_1665 {ECO:0000313|EMBL:ACB90917.1};
OS   Streptococcus pneumoniae (strain CGSP14).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=516950 {ECO:0000313|EMBL:ACB90917.1, ECO:0000313|Proteomes:UP000001682};
RN   [1] {ECO:0000313|EMBL:ACB90917.1, ECO:0000313|Proteomes:UP000001682}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGSP14 {ECO:0000313|EMBL:ACB90917.1,
RC   ECO:0000313|Proteomes:UP000001682};
RX   PubMed=19361343; DOI=10.1186/1471-2164-10-158;
RA   Ding F., Tang P., Hsu M.-H., Cui P., Hu S., Yu J., Chiu C.-H.;
RT   "Genome evolution driven by host adaptations results in a more virulent and
RT   antimicrobial-resistant Streptococcus pneumoniae serotype 14.";
RL   BMC Genomics 10:158-158(2009).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC       {ECO:0000256|ARBA:ARBA00009348}.
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DR   EMBL; CP001033; ACB90917.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2IRU8; -.
DR   CAZy; CBM40; Carbohydrate-Binding Module Family 40.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   KEGG; spw:SPCG_1665; -.
DR   HOGENOM; CLU_002070_0_0_9; -.
DR   Proteomes; UP000001682; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.120.10.10; -; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR004124; Glyco_hydro_33_N.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR023364; Trans_sialidase_dom3.
DR   InterPro; IPR005877; YSIRK_signal_dom.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
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; PF02973; Sialidase; 1.
DR   Pfam; PF04650; YSIRK_signal; 1.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50939; Sialidases; 1.
DR   PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        32..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          948..980
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|PROSITE:PS50847"
FT   REGION          57..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  109129 MW;  1EB4EDCC0FD82273 CRC64;
     MSYFRNRDID IERISMNRSV QERKCRYSIR KLSVGAVSMI VGAVVFGTSP VLAQEGASEQ
     PLANETQLSG ESSTLTDTEK SQPSSETELS GNKQEQERKD KQEEKIPRDY YARDLENVET
     VIEKEDVETN ASNGQRVDLS SELDKLKKLE NATVHMEFKP DAKAPAFYNL FSVSSATKKD
     EYFTMAVYNN TATLEGRGSD GQQFYGNYND APLKVKPGQW NSVTFTVEKP TAELPKGRVR
     LYVNGVLSRT SLKSGNFIKD MPDVTHVQIG ATKRANNTVW GSNLQIQNLT VYNRALTPEE
     VQKRSQLFKR SDLEKKLPEG AVLTEKTDIF ESGRNGKPNK DGIKSYRIPA LLKTDKGTLI
     AGADERRLHS SDWGDIGMVI RRSEDNGKTW GDKVVISNLR DNPEAKDPAA PSPLNIDMVL
     VQDPTTKRIF SIYDMFPEGR AVFGMPKTPE KAYEKIGDKT YQILYKQGES GHYTVRENGE
     VYNAQNQKTD YRVVVNPTEP GYRDKGNLYK GQELIGNIYF AHSTKNPFRV ANTSYLWMSY
     SDDDGKTWSA PRDITPGLRK DWMKFLGTGP GTGIVLRNGP HKGRILIPVY TTNNVSHLNG
     SQSSRVIYSD DHGKTWHAGE AVNDNRQVDG QKIHSSTMNN ERAQNTESTV VQLNNGDVKL
     FMRGLTGDLQ VATSKDGGVT WEKDIKRYPQ VKDVYVQMSA IHTMHEGKEY IILSNAGGPK
     RENGMVHLAR VEENGELTWL KHNPIQKGEF AYNSLQELGN GEYGILYEHT EKGQNAYTLS
     FRKFNWDFLS KDLISPTEAK VKRTREMGKG EMGKGVIGLE FDSEVLVNKA PTLQLANGKT
     ATFLTQYDSK TLLFAVDKED IGQEIIGIAK GSIESMHNLP VNLAGARVPG GVNGSKAAVH
     EVPEFTGGVN GTEPAVHEIA EYKGSDSLVT LTTKEDYTYK APLAQQALPE TGNKESDLLA
     SLGLTAFFLG LFTLGKKREQ
//