ID A4UUQ0_9VIRU Unreviewed; 811 AA.
AC A4UUQ0;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=PK1A endosialidase {ECO:0000313|EMBL:ABP02011.1};
DE EC=3.2.1.129 {ECO:0000313|EMBL:ABP02011.1};
OS Enterobacteria phage K1A.
OC Viruses.
OX NCBI_TaxID=435637 {ECO:0000313|EMBL:ABP02011.1};
RN [1] {ECO:0000313|EMBL:ABP02011.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=A {ECO:0000313|EMBL:ABP02011.1};
RX PubMed=17394421; DOI=10.1042/BJ20070177;
RA Jakobsson E., Jokilammi A., Aalto J., Ollikka P., Lehtonen J.V.,
RA Hirvonen H., Finne J.;
RT "Identification of amino acid residues at the active site of endosialidase
RT that dissociate the polysialic acid binding and cleaving activities in
RT Escherichia coli K1 bacteriophages.";
RL Biochem. J. 405:465-472(2007).
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DR EMBL; EF507428; ABP02011.1; -; Genomic_DNA.
DR CAZy; GH58; Glycoside Hydrolase Family 58.
DR BRENDA; 3.2.1.129; 9456.
DR GO; GO:0016996; F:endo-alpha-(2,8)-sialidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd10144; Peptidase_S74_CIMCD; 1.
DR Gene3D; 2.120.10.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 4.10.1090.10; Endosialidase, domain 4; 1.
DR Gene3D; 3.30.750.60; Endosialidase, N-terminal extension domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 Pfam; PF13884; Peptidase_S74; 1.
DR PRINTS; PR00849; GLHYDRLASE58.
DR SUPFAM; SSF69349; Phage fibre proteins; 1.
DR SUPFAM; SSF50939; Sialidases; 1.
DR PROSITE; PS51688; ICA; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000313|EMBL:ABP02011.1};
KW Hydrolase {ECO:0000313|EMBL:ABP02011.1}.
FT DOMAIN 706..808
FT /note="Peptidase S74"
FT /evidence="ECO:0000259|PROSITE:PS51688"
SQ SEQUENCE 811 AA; 90352 MW; 255936E7388C30A0 CRC64;
MIQRLSSSLV KFKSKIAGAI WRNLDDKLTE VVSLKDFGAK GDGKTNDQDA VNAAMASGKR
IDGAGATYKV SSLPDMERFY NTRFVWERLS GQPLYYVSKG FINGELYKIT DNPYYNAWPQ
DKAFVYENVI YAPYMGSDRH GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM
SMGVCRNRLF AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG
LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN WHMGTSFHKS
PWRKTDLGLI PHVTEVHSFA TIDNNGFVMG YHQGDVAPRE VGLFYFPDAF NSPSNYVRRQ
IPSEYEPDAA EPCIKYYDGV LYLITRGTRG DRLGSSLHRS RDIGQTWESL RFPHNVHHTT
LPFAKVGDDL IMFGSERAEN EWEAGAPDDR YKASYPRTFY ARLNVNNWNA ADIEWVNITD
QIYQGDIVNS SVGVGSVVVK DSYIYYIFGG ENHFNPMTYG DNRDKDPFKG HGHPTDIYCY
KMQIANDSRV SRKFTYGATP GQAIPTFMGT DGIRTIPAPL HLSGEVVAAD MTVEHLTLKA
STSANIRSEM LMEREYGFIG KTIPKDNPTA QRVIISGGGG TAADTGAQIT LHGAGSSTSR
RAVYNANEHL FQSGAIMPYN DNVYPAGGPR NRFTTIHLTS DPIITSDATH KYGSQGIDES
VLKAWGKVSF KQYKLIGEMS RGVHHTHFGV LAQDIVAAFA SEGLDAIDFG IVSFEEGQFG
VRYSEILILE AAYTRYRLDK LEEMYATNKI S
//
