ID NANA_STREE Reviewed; 1035 AA. AC P62575; Q54722; Q59959; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 1. DT 13-SEP-2023, entry version 109. DE RecName: Full=Sialidase A; DE EC=3.2.1.18; DE AltName: Full=Neuraminidase A; DE Flags: Precursor; GN Name=nanA; OS Streptococcus pneumoniae. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1313; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=R36A / NCTC 10319; RX PubMed=8063384; DOI=10.1128/iai.62.9.3688-3695.1994; RA Camara M., Boulnois G.J., Andrew P.W., Mitchell T.J.; RT "A neuraminidase from Streptococcus pneumoniae has the features of a RT surface protein."; RL Infect. Immun. 62:3688-3695(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 882-1035. RC STRAIN=Serotype 6; RX PubMed=8759848; DOI=10.1128/jb.178.16.4854-4860.1996; RA Berry A.M., Lock R.A., Paton J.C.; RT "Cloning and characterization of nanB, a second Streptococcus pneumoniae RT neuraminidase gene, and purification of the NanB enzyme from recombinant RT Escherichia coli."; RL J. Bacteriol. 178:4854-4860(1996). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha- CC (2->8)- glycosidic linkages of terminal sialic acid residues in CC oligosaccharides, glycoproteins, glycolipids, colominic acid and CC synthetic substrates.; EC=3.2.1.18; CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE- CC ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00477}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X72967; CAA51473.1; -; Genomic_DNA. DR EMBL; U43526; AAC44391.1; -; Genomic_DNA. DR PIR; T30287; T30287. DR PDB; 2VVZ; X-ray; 2.50 A; A/B=319-822. DR PDB; 2YA4; X-ray; 1.80 A; A/B=318-791. DR PDB; 2YA5; X-ray; 2.00 A; A/B=318-791. DR PDB; 2YA6; X-ray; 2.00 A; A/B=318-791. DR PDB; 2YA7; X-ray; 1.89 A; A/B/C/D=318-791. DR PDB; 2YA8; X-ray; 1.75 A; A/B=318-791. DR PDB; 4C1X; X-ray; 1.84 A; A=121-305. DR PDB; 4ZXK; X-ray; 1.84 A; A/B=121-305. DR PDB; 5KKY; X-ray; 2.39 A; A/B=318-792. DR PDB; 7A54; X-ray; 2.70 A; A/B=318-791. DR PDB; 7A5X; X-ray; 1.94 A; A/B=318-791. DR PDBsum; 2VVZ; -. DR PDBsum; 2YA4; -. DR PDBsum; 2YA5; -. DR PDBsum; 2YA6; -. DR PDBsum; 2YA7; -. DR PDBsum; 2YA8; -. DR PDBsum; 4C1X; -. DR PDBsum; 4ZXK; -. DR PDBsum; 5KKY; -. DR PDBsum; 7A54; -. DR PDBsum; 7A5X; -. DR AlphaFoldDB; P62575; -. DR SMR; P62575; -. DR BindingDB; P62575; -. DR ChEMBL; CHEMBL4105839; -. DR CAZy; CBM40; Carbohydrate-Binding Module Family 40. DR CAZy; GH33; Glycoside Hydrolase Family 33. DR BRENDA; 3.2.1.18; 1960. DR SABIO-RK; P62575; -. DR EvolutionaryTrace; P62575; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0052794; F:exo-alpha-(2->3)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052795; F:exo-alpha-(2->6)-sialidase activity; IEA:UniProtKB-EC. DR GO; GO:0052796; F:exo-alpha-(2->8)-sialidase activity; IEA:UniProtKB-EC. 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 1: Evidence at protein level; KW 3D-structure; Cell wall; Glycosidase; Hydrolase; Peptidoglycan-anchor; KW Repeat; Secreted; Signal. FT SIGNAL 1..53 FT /evidence="ECO:0000255" FT CHAIN 54..1006 FT /note="Sialidase A" FT /id="PRO_0000012034" FT PROPEP 1007..1035 FT /note="Removed by sortase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT /id="PRO_0000012035" FT REPEAT 381..392 FT /note="BNR 1" FT REPEAT 539..550 FT /note="BNR 2" FT REPEAT 607..618 FT /note="BNR 3" FT REPEAT 672..683 FT /note="BNR 4" FT REGION 57..112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 902..951 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1003..1007 FT /note="LPXTG sorting signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" 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" FT ACT_SITE 372 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 647 FT /evidence="ECO:0000250" FT BINDING 347 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 663 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 1006 FT /note="Pentaglycyl murein peptidoglycan amidated threonine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477" FT STRAND 121..129 FT /evidence="ECO:0007829|PDB:4C1X" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 136..138 FT /evidence="ECO:0007829|PDB:4C1X" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:4C1X" FT HELIX 143..147 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 150..160 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 166..174 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 191..197 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 221..228 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:4C1X" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 266..274 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 284..294 FT /evidence="ECO:0007829|PDB:4C1X" FT HELIX 298..303 FT /evidence="ECO:0007829|PDB:4C1X" FT STRAND 327..330 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 345..353 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 359..368 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 370..385 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:7A5X" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 414..422 FT /evidence="ECO:0007829|PDB:2YA8" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 429..436 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 453..456 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 459..466 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 473..475 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 477..479 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 488..493 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 500..502 FT /evidence="ECO:0007829|PDB:2YA8" FT TURN 503..506 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 507..510 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 513..517 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 525..529 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 535..543 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 555..558 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 563..568 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 570..572 FT /evidence="ECO:0007829|PDB:7A54" FT TURN 580..583 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 585..593 FT /evidence="ECO:0007829|PDB:2YA8" FT TURN 594..596 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 597..600 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 603..611 FT /evidence="ECO:0007829|PDB:2YA8" FT TURN 622..625 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 626..628 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 631..633 FT /evidence="ECO:0007829|PDB:2YA8" FT TURN 635..637 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 641..643 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 647..652 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 658..662 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 665..680 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 686..692 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 699..705 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 708..716 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 718..731 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 733..735 FT /evidence="ECO:0007829|PDB:2VVZ" FT STRAND 737..749 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 753..759 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 762..769 FT /evidence="ECO:0007829|PDB:2YA8" FT STRAND 778..785 FT /evidence="ECO:0007829|PDB:2YA8" FT HELIX 786..790 FT /evidence="ECO:0007829|PDB:2YA8" SQ SEQUENCE 1035 AA; 114742 MW; C5B8A2D7A12E12F3 CRC64; MSYFRNRDID IERNSMNRSV QERKCRYSIR KLSVGAVSMI VGAVVFGTSP VLAQEGASEQ PLANETQLSG ESSTLTDTEK SQPSSETELS GNKQEQERKD KQEEKIPRDY YARDLENVET VIEKEDVETN ASNGQRVDLS SELDKLKKLE NATVHMEFKP DAKAPAFYNL FSVSSATKKD EYFTMAVYNN TATLEGRGSD GKQFYNNYND APLKVKPGQW NSVTFTVEKP TAELPKGRVR LYVNGVLSRT SLRSGNFIKD MPDVTHVQIG ATKRANNTVW GSNLQIRNLT VYNRALTPEE VQKRSQLFKR SDLEKKLPEG AALTEKTDIF ESGRNGKPNK DGIKSYRIPA LLKTDKGTLI AGADERRLHS SDWGDIGMVI RRSEDNGKTW GDRVTITNLR DNPKASDPSI GSPVNIDMVL VQDPETKRIF SIYDMFPEGK GIFGMSSQKE EAYKKIDGKT YQILYREGEK GAYTIRENGT VYTPDGKATD YRVVVDPVKP AYSDKGDLYK GNQLLGNIYF TTNKTSPFRI AKDSYLWMSY SDDDGKTWSA PQDITPMVKA DWMKFLGVGP GTGIVLRNGP HKGRILIPVY TTNNVSHLNG SQSSRIIYSD DHGKTWHAGE AVNDNRQVDG QKIHSSTMNN RRAQNTESTV VQLNNGDVKL FMRGLTGDLQ VATSKDGGVT WEKDIKRYPQ VKDVYVQMSA IHTMHEGKEY IILSNAGGPK RENGMVHLAR VEENGELTWL KHNPIQKGEF AYNSLQELGN GEYGILYEHT EKGQNAYTLS FRKFNWDFLS KDLISPTEAK VKRTREMGKG VIGLEFDSEV LVNKAPTLQL ANGKTARFMT QYDTKTLLFT VDSEDMGQKV TGLAEGAIES MHNLPVSVAG TKLSNGMNGS EAAVHEVPEY TGPLGTSGEE PAPTVEKPEY TGPLGTSGEE PAPTVEKPEY TGPLGTAGEE AAPTVEKPEF TGGVNGTEPA VHEIAEYKGS DSLVTLTTKE DYTYKAPLAQ QALPETGNKE SDLLASLGLT AFFLGLFTLG KKREQ //