ID   ENAN_BPK1E              Reviewed;         811 AA.
AC   P49714;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   14-APR-2009, entry version 48.
DE   RecName: Full=Endo-N-acetylneuraminidase;
DE            Short=Endo-N;
DE            EC=3.2.1.129;
DE   AltName: Full=Endosialidase;
GN   Name=GP90; Synonyms=END;
OS   Enterobacteria phage K1E (Bacteriophage K1E).
OC   Viruses; dsDNA viruses, no RNA stage; Caudovirales; Podoviridae;
OC   Autographivirinae.
OX   NCBI_TaxID=344022;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE OF
RP   1-6; 330-349 AND 613-632.
RC   STRAIN=ATCC 40221;
RX   MEDLINE=95351985; PubMed=7626018;
RA   Long G.S., Bryant J.M., Taylor P.W., Luzio J.P.;
RT   "Complete nucleotide sequence of the gene encoding bacteriophage E
RT   endosialidase: implications for K1E endosialidase structure and
RT   function.";
RL   Biochem. J. 309:543-550(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gerardy-Schahn R., Hansen A., Brennecke T., Muehlenhoff M.,
RA   Eckhardt M., Ziesing S., Lottspeich F., Frosch M.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE REVISION TO 53-56; 523 AND 539.
RA   Muehlenhoff M.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for initial absorption of the phage to the
CC       host bacterium. Degradation of the alpha-2,8-linked polysialic
CC       acid K1 capsule.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (2->8)-alpha-sialosyl
CC       linkages in oligo- or poly(sialic) acids.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 58 family.
CC   -!- SIMILARITY: Contains 3 BNR repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X78310; CAA55120.1; -; Genomic_DNA.
DR   EMBL; Z36986; CAA85449.2; -; Genomic_DNA.
DR   CAZy; GH58; Glycoside Hydrolase Family 58.
DR   GO; GO:0016996; F:endo-alpha-sialidase activity; IEA:EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001724; Glyco_hydro_58.
DR   PRINTS; PR00849; GLHYDRLASE58.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Repeat.
FT   CHAIN         1    811       Endo-N-acetylneuraminidase.
FT                                /FTId=PRO_0000057708.
FT   REPEAT      150    161       BNR 1.
FT   REPEAT      286    293       BNR 2.
FT   REPEAT      398    409       BNR 3.
FT   COMPBIAS    642    645       Poly-Ser.
SQ   SEQUENCE   811 AA;  90524 MW;  8F96F465ED533B6E CRC64;
     MIQRLGSSLV KFKSKIAGAI WRNLDDKLTE VVSLKDFGAK GDGKTNDQDA VNAAMASGKR
     IDGAGATYKV SSLPDMERFY NTRFVWERLA GQPLYYVSKG FINGELYKIT DNPYYNAWPQ
     DKAFVYENVI YAPYMGSDRH GVSRLHVSWV KSGDDGQTWS TPEWLTDMHP DYPTVNYHCM
     SMGVCRNRLF AMIETRTLAK NELTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG
     LFVGDFVNFS NSAVTGVSGD MKVATVIDKD NFTVLTPNQQ TSDLNNAGKN WHMGTSFHKS
     PWRKTDLGLI PRVTEVHSFA TIDNNGFVMG YHQGDVAPRE VGLFYFPDAF NSPSNYVRRQ
     IPSEYEPDAA EPCIKYYDGV LYLITRGTRG DRLGSSLHRS RDIGQTWESL RFPHNVHHTT
     LPFAKVGDDL IMFGSERAEN EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD
     QIYQGDIVNS SVGVGSVVVK DSFIYYIFGG ENHFNPMTYG DNKDKDPFKG HGHPTDIYCY
     KMQIANDNRV SRKFTYGATP GQAIPTFMGT DGIRNIPAPL YFSDNIVTED TKVGHLTLKA
     STSANIRSEM QMEGEYGFIG KSVPKDKPTG QRLIICGGEG TSSSSGAQIT LHGSNSSNAK
     RITYNGNEHL FQGAPIMPAV DNQFAAGGPS NRFTTIYLGS DPVTTSDADH KYGISSINTK
     VLKAWSRVGF KQYGLNSEAE RNLDSIHFGV LAQDIVAAFE AEGLDAIKYG IVSFEEGRYG
     VRYSEVLILE AAYTRHRLDK LEEMYATNKI S
//