ID I7HXG2_9CAUD Unreviewed; 918 AA.
AC I7HXG2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Phi92_gp143 {ECO:0000313|EMBL:CBY99572.1};
DE EC=3.2.1.129 {ECO:0000313|EMBL:CBY99572.1};
DE Flags: Precursor;
GN Name=PHI92_gene_143 {ECO:0000313|EMBL:CBY99572.1};
GN ORFNames=PHI92_143 {ECO:0000313|EMBL:CBY99572.1};
OS Escherichia phage phi92.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Stephanstirmvirinae; Justusliebigvirus; Justusliebigvirus phi92.
OX NCBI_TaxID=948870 {ECO:0000313|EMBL:CBY99572.1, ECO:0000313|Proteomes:UP000009013};
RN [1] {ECO:0000313|EMBL:CBY99572.1, ECO:0000313|Proteomes:UP000009013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35860-B1 {ECO:0000313|EMBL:CBY99572.1};
RX PubMed=6401818;
RA Kwiatkowski B., Boschek B., Thiele H., Stirm S.;
RT "Substrate specificity of two bacteriophage-associated endo-N-
RT acetylneuraminidases.";
RL J. Virol. 45:367-374(1983).
RN [2] {ECO:0000313|EMBL:CBY99572.1, ECO:0000313|Proteomes:UP000009013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35860-B1 {ECO:0000313|EMBL:CBY99572.1};
RX PubMed=3298958; DOI=10.1016/0076-6879(87)38067-X;
RA Kwiatkowski B., Stirm S.;
RT "Polysialic acid depolymerase.";
RL Methods Enzymol. 138:786-792(1987).
RN [3] {ECO:0000313|EMBL:CBY99572.1, ECO:0000313|Proteomes:UP000009013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35860-B1 {ECO:0000313|EMBL:CBY99572.1};
RX PubMed=22787233; DOI=10.1128/JVI.00801-12;
RA Schwarzer D., Buettner F.F., Browning C., Nazarov S., Rabsch W., Bethe A.,
RA Oberbeck A., Bowman V.D., Stummeyer K., Leiman P.G., Muhlenhoff M.,
RA Gerardy-Schahn R.;
RT "A Multivalent Adsorption Apparatus Explains the Broad Host Range of Phage
RT phi92: a Comprehensive Genomic and Structural Analysis.";
RL J. Virol. 86:10384-10398(2012).
RN [4] {ECO:0000313|Proteomes:UP000009013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22325780; DOI=10.1016/j.str.2011.12.009;
RA Browning C., Shneider M.M., Bowman V.D., Schwarzer D., Leiman P.G.;
RT "Phage pierces the host cell membrane with the iron-loaded spike.";
RL Structure 20:326-339(2012).
RN [5] {ECO:0007829|PDB:4HIZ}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 76-756 IN COMPLEX WITH CALCIUM.
RA Schwarzer D., Browning C., Oberbeck A., Stummeyer K., Muhlenhoff M.,
RA Gerardy-Schahn R., Leiman P.G.;
RT "Crystal Structure of Endosialidase from Phage phi92 that cleaves
RT alpha2,8- and alpha2,9-linked polysialic acid.";
RL Submitted (OCT-2012) to the PDB data bank.
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DR EMBL; FR775895; CBY99572.1; -; Genomic_DNA.
DR RefSeq; YP_009012475.1; NC_023693.1.
DR PDB; 4HIZ; X-ray; 1.60 A; A/B/C=76-756.
DR PDBsum; 4HIZ; -.
DR SMR; I7HXG2; -.
DR GeneID; 22277995; -.
DR KEGG; vg:22277995; -.
DR OrthoDB; 303at10239; -.
DR BRENDA; 3.2.1.129; 13984.
DR Proteomes; UP000009013; Genome.
DR GO; GO:0098015; C:virus tail; IEA:UniProtKB-KW.
DR GO; GO:0016996; F:endo-alpha-(2,8)-sialidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 1.20.5.1240; Endo-n-acetylneuraminidase; 1.
DR Gene3D; 3.30.2460.10; Endo-n-acetylneuraminidase domain; 1.
DR Gene3D; 4.10.1090.10; Endosialidase, domain 4; 1.
DR Gene3D; 3.30.750.60; Endosialidase, N-terminal extension 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 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:4HIZ}; Calcium {ECO:0007829|PDB:4HIZ};
KW Glycosidase {ECO:0000313|EMBL:CBY99572.1};
KW Hydrolase {ECO:0000313|EMBL:CBY99572.1};
KW Metal-binding {ECO:0007829|PDB:4HIZ};
KW Reference proteome {ECO:0000313|Proteomes:UP000009013};
KW Viral tail protein {ECO:0000256|ARBA:ARBA00022732};
KW Virion {ECO:0000256|ARBA:ARBA00022732}.
FT DOMAIN 757..918
FT /note="Peptidase S74"
FT /evidence="ECO:0000259|PROSITE:PS51688"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4HIZ"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4HIZ"
FT BINDING 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:4HIZ"
FT BINDING 586
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4HIZ"
FT BINDING 588
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4HIZ"
FT BINDING 589
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:4HIZ"
SQ SEQUENCE 918 AA; 102380 MW; B3B5AA4D64BB03CE CRC64;
MSTTITNLPE TSKVNSSDYL VLDQPDKTVK STVSNFLADT GVVLATQLKD TSGATKYPEL
QMSRWRDEGD PRGWGAVGDG ATDDTNAITQ LLAAMPDGWI IDGRNLTFKV TTLPDISKFK
NAAFVYERIV GQPLTYVSEG FFDGNLTKIT DTPFYNAWTQ DKTFVYDNVI YAPFMAGERH
GVQNLHVAWV KSGDDGQTWS MPEWLTPIHP DYTADKVNYH CMSMGVCGNR LYAVIETRYL
SNMRLKKAEL WSRPMPYYRR PTGGITISSG STTATIVLKK HGLKVGDAVN FSNSGATGVS
GNMTVASVIN KDTFTVTLAR AATSNIDNTG TTWHFGTRFW DSPWEITELP DVAYSTNADL
CVTETHSFTV IDDDNYTFAV GYHNGDISPR RLGILYFNNA YSDPSSFTRR TISQEYADNA
AEPCIKYYDG ILYLTTRGTS TSAAGSTLAM SADLGENWNY LRFPNNVHHT NLPFAKVGDY
LYIFGTERSF GEWEGQELDN RYKGTYPRTF MCKINVSSWP VSLSNVQWFN ITDQIYQGHI
VNSACGVGSV CVKDGWLYYI FGGEDFLSPW SIGDNSKKLW YKHDGHPADL YSYRLKITEH
DFVSRDFKYG ATPNRTLPVS MGTDGVRHVS APVTFDNDVQ MYSLTVTGLE HDGTQQSAVR
VKLDGDYGVI AKNIPIKNPS EQRLILCGGE TPYTTDGSLL QLYGSNHTYP NRAILYAPGG
AYTQNNFMPY LDGQVSLGGA SNRWSEVYAS TGTINTSDGT LKTKPTEIED ILLKAWEDIH
VISYQWLSAV AEKGDSARIH FGVIAQDVRD ILINYGLMDE NSTDCKYAFL CYDEYPAMYD
SVVTGQKEIT LLDDEGNNVI DEEGNPVTIV EDVVETIEVI PAGSRWGIRA DQMFFIEMAY
QRKKLKALEE RLATLESK
//
