ID   FIBER_BPK1E             Reviewed;         811 AA.
AC   P49714;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Tail spike protein {ECO:0000305};
DE            Short=TSP;
DE   AltName: Full=Endo-N-acetylneuraminidase;
DE            Short=Endo-N;
DE            EC=3.2.1.129;
DE   AltName: Full=Endo-alpha-sialidase {ECO:0000305};
DE   AltName: Full=EndoNE;
DE   Contains:
DE     RecName: Full=C-terminal chaperone protein;
GN   Name=GP90; Synonyms=END;
OS   Escherichia phage K1E (Bacteriophage K1E).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Molineuxvirinae; Vectrevirus.
OX   NCBI_TaxID=344022;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6; 330-349 AND
RP   613-632.
RC   STRAIN=ATCC 40221;
RX   PubMed=7626018; DOI=10.1042/bj3090543;
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 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., Eckhardt M.,
RA   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: [Tail spike protein]: Responsible for initial absorption of
CC       the phage to the host bacterium. Degrades the alpha-2,8-linked
CC       polysialic acid K1 capsule by cleaving within the polymer chain of
CC       polysialic acid. {ECO:0000250|UniProtKB:Q04830}.
CC   -!- FUNCTION: [C-terminal chaperone protein]: The C-terminal chaperone
CC       protein mediates homotrimerization and proper folding of the catalytic
CC       endo-N trimer. {ECO:0000250|UniProtKB:Q04830}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or
CC         poly(sialic) acids.; EC=3.2.1.129;
CC         Evidence={ECO:0000250|UniProtKB:Q04830};
CC   -!- SUBUNIT: [Tail spike protein]: Homotrimer. Interacts with sialic acid.
CC       {ECO:0000250|UniProtKB:Q04830}.
CC   -!- SUBCELLULAR LOCATION: [Tail spike protein]: Virion. Note=Tail spike.
CC       {ECO:0000250|UniProtKB:Q04830}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: Proteolytic cleavage and release of the chaperone stabilizes the
CC       folded protein. {ECO:0000250|UniProtKB:Q04830}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 58 family. {ECO:0000305}.
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DR   EMBL; X78310; CAA55120.1; -; Genomic_DNA.
DR   EMBL; Z36986; CAA85449.2; -; Genomic_DNA.
DR   SMR; P49714; -.
DR   CAZy; GH58; Glycoside Hydrolase Family 58.
DR   BioCyc; MetaCyc:MON-20295; -.
DR   GO; GO:0098024; C:virus tail, fiber; IEA:UniProtKB-KW.
DR   GO; GO:0016996; F:endo-alpha-(2,8)-sialidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098996; P:disruption of host cell glycocalyx during viral entry; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 4.10.1090.10; -; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR024427; Endosialidase_beta_barrel.
DR   InterPro; IPR024428; Endosialidase_beta_prop.
DR   InterPro; IPR024430; Endosialidase_C_dom.
DR   InterPro; IPR044914; Endosialidase_C_dom_sf.
DR   InterPro; IPR024429; Endosialidase_N-extension.
DR   InterPro; IPR001724; Glycl_Hydrolase_58.
DR   InterPro; IPR030392; S74_ICA.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF12195; End_beta_barrel; 1.
DR   Pfam; PF12217; End_beta_propel; 1.
DR   Pfam; PF12218; End_N_terminal; 1.
DR   Pfam; PF12219; End_tail_spike; 1.
DR   PRINTS; PR00849; GLHYDRLASE58.
DR   SUPFAM; SSF50939; SSF50939; 1.
DR   PROSITE; PS51688; ICA; 1.
PE   1: Evidence at protein level;
KW   Degradation of host capsule during virus entry;
KW   Degradation of host cell envelope components during virus entry;
KW   Direct protein sequencing; Glycosidase; Host-virus interaction; Hydrolase;
KW   Repeat; Viral attachment to host adhesion receptor;
KW   Viral attachment to host cell; Viral tail fiber protein;
KW   Viral tail protein; Virion; Virus entry into host cell.
FT   CHAIN           1..811
FT                   /note="Tail spike protein"
FT                   /id="PRO_0000057708"
FT   CHAIN           707..811
FT                   /note="C-terminal chaperone protein"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT                   /id="PRO_0000438181"
FT   REPEAT          150..161
FT                   /note="BNR 1"
FT   REPEAT          286..293
FT                   /note="BNR 2"
FT   REPEAT          398..409
FT                   /note="BNR 3"
FT   DOMAIN          706..808
FT                   /note="Peptidase S74"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   ACT_SITE        386
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   ACT_SITE        437
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   SITE            332
FT                   /note="Binding to sialic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   SITE            335
FT                   /note="Binding to sialic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   SITE            339
FT                   /note="Binding to sialic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   SITE            368
FT                   /note="Binding to sialic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   SITE            388
FT                   /note="Binding to sialic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
FT   SITE            389
FT                   /note="Binding to sialic acid"
FT                   /evidence="ECO:0000250|UniProtKB:Q04830"
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