ID   NANH_PAESO              Reviewed;         404 AA.
AC   P15698;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Sialidase;
DE            EC=3.2.1.18;
DE   AltName: Full=Neuraminidase;
DE   Flags: Precursor;
OS   Paeniclostridium sordellii (Clostridium sordellii).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Paeniclostridium.
OX   NCBI_TaxID=1505;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 28-45.
RC   STRAIN=ATCC 9714 / DSM 2141 / JCM 3814 / LMG 15708 / NCIMB 10717;
RX   PubMed=2693593; DOI=10.1099/00221287-135-11-3087;
RA   Rothe B., Roggentin P., Frank R., Bloecker H., Schauer R.;
RT   "Cloning, sequencing and expression of a sialidase gene from Clostridium
RT   sordellii G12.";
RL   J. Gen. Microbiol. 135:3087-3096(1989).
CC   -!- FUNCTION: Sialidases have been suggested to be pathogenic factors in
CC       microbial infections.
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.
CC   -!- PTM: It is possible that the sialidase is cleaved in front of a
CC       cysteine within the leader peptide, forming a glyceride thioether bond
CC       which links the protein to the membrane. A second proteolytic cleavage
CC       releases the mature extracellular protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family. {ECO:0000305}.
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DR   EMBL; M31584; AAA23280.1; -; Genomic_DNA.
DR   PIR; A37234; A37234.
DR   AlphaFoldDB; P15698; -.
DR   SMR; P15698; -.
DR   STRING; 1292035.H476_2657; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   eggNOG; COG4409; Bacteria.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011040; Sialidase.
DR   InterPro; IPR026856; Sialidase_fam.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR008377; Sialidase_trypan.
DR   PANTHER; PTHR10628; PTHR10628; 1.
DR   Pfam; PF13859; BNR_3; 1.
DR   PRINTS; PR01803; TCSIALIDASE.
DR   SUPFAM; SSF50939; SSF50939; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:2693593"
FT   CHAIN           28..404
FT                   /note="Sialidase"
FT                   /id="PRO_0000012030"
FT   REPEAT          89..100
FT                   /note="BNR 1"
FT   REPEAT          158..169
FT                   /note="BNR 2"
FT   REPEAT          226..237
FT                   /note="BNR 3"
FT   REPEAT          273..284
FT                   /note="BNR 4"
FT   ACT_SITE        80
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        365
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         263
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  44729 MW;  525B9DA90083AA6A CRC64;
     MKKFIKILKV LSMAIVLSAC NINGIFASNL NTTNEPQKTT VFNKNDNTWN AQYFRIPSLQ
     TLADGTMLAF SDIRYNGAED HAYIDIGAAK STDNGQTWDY KTVMENDRID STFSRVMDST
     TVVTDTGRII LIAGSWNKNG NWASSTTSLR SDWSVQMVYS DDNGETWSDK VDLTTNKARI
     KNQPSNTIGW LAGVGSGIVM SDGTIVMPIQ IALRENNANN YYSSVIYSKD NGETWTMGNK
     VPDPKTSENM VIELDGALIM SSRNDGKNYR ASYISYDMGS TWEVYDPLHN KISTGNGSGC
     QGSFIKVTAK DGHRLGFISA PKNTKGGYVR DNITVYMIDF DDLSKGIREL CSPYPEDGNS
     SGGGYSCLSF NDGKLSILYE ANGNIEYKDL TDYYLSIENN KKLK