NANA_STREE
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 03-AUG-2022, entry version 104.
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; Firmicutes; 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}.
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DR EMBL; X72967; CAA51473.1; -; Genomic_DNA.
DR EMBL; U43526; AAC44391.1; -; Genomic_DNA.
DR PIR; T30287; T30287.
DR RefSeq; WP_010976603.1; NZ_FHUZ01000001.1.
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 Gene3D; 2.40.220.10; -; 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 PANTHER; PTHR10628; PTHR10628; 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; SSF49899; 1.
DR SUPFAM; SSF50939; SSF50939; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 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
