NEEDL_BPT4
ID NEEDL_BPT4 Reviewed; 575 AA.
AC P16009;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Pre-baseplate central spike protein Gp5 {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000303|PubMed:10217762, ECO:0000303|PubMed:27193680};
DE Short=Pre-Gp5 {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000303|PubMed:16956798};
DE AltName: Full=Peptidoglycan hydrolase gp5 {ECO:0000255|HAMAP-Rule:MF_04151};
DE EC=3.2.1.17 {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:10217762, ECO:0000269|PubMed:3157805};
DE Contains:
DE RecName: Full=Baseplate central spike protein Gp5* {ECO:0000255|HAMAP-Rule:MF_04151};
DE AltName: Full=Mature Gp5 {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000303|PubMed:16956798};
DE Contains:
DE RecName: Full=Gp5C {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000303|PubMed:16956798};
GN Name=5 {ECO:0000255|HAMAP-Rule:MF_04151};
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2488704;
RA Mosig G., Lin G.W., Franklin J., Fan W.H.;
RT "Functional relationships and structural determinants of two bacteriophage
RT T4 lysozymes: a soluble (gene e) and a baseplate-associated (gene 5)
RT protein.";
RL New Biol. 1:171-179(1989).
RN [2]
RP SEQUENCE REVISION.
RA Mosig G.;
RL Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RX PubMed=2740234; DOI=10.1093/nar/17.11.4392;
RA Koch T., Lamm N., Rueger W.;
RT "Sequencing, cloning and overexpression of genes of bacteriophage T4
RT between map positions 74.325 and 77.184.";
RL Nucleic Acids Res. 17:4392-4392(1989).
RN [5]
RP PROTEIN SEQUENCE OF 1-7 AND 352-358, PROTEOLYTIC CLEAVAGE (BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5 PRECURSOR), SUBCELLULAR LOCATION (BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5*), SUBCELLULAR LOCATION (GP5C), AND CATALYTIC
RP ACTIVITY (BASEPLATE CENTRAL SPIKE PROTEIN GP5*).
RX PubMed=10217762; DOI=10.1128/jb.181.9.2739-2744.1999;
RA Kanamaru S., Gassner N.C., Ye N., Takeda S., Arisaka F.;
RT "The C-terminal fragment of the precursor tail lysozyme of bacteriophage T4
RT stays as a structural component of the baseplate after cleavage.";
RL J. Bacteriol. 181:2739-2744(1999).
RN [6]
RP PROTEIN SEQUENCE OF 1-6 AND 386-390, PROTEOLYTIC CLEAVAGE (BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5 PRECURSOR), SUBCELLULAR LOCATION (BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5*), AND SUBCELLULAR LOCATION (GP5C).
RX PubMed=15342608; DOI=10.1128/jb.186.18.6335-6339.2004;
RA Ye N., Nemoto N.;
RT "Processing of the tail lysozyme (gp5) of bacteriophage T4.";
RL J. Bacteriol. 186:6335-6339(2004).
RN [7]
RP FUNCTION (BASEPLATE CENTRAL SPIKE PROTEIN GP5*), BIOPHYSICOCHEMICAL
RP PROPERTIES (BASEPLATE CENTRAL SPIKE PROTEIN GP5*), AND CATALYTIC ACTIVITY
RP (BASEPLATE CENTRAL SPIKE PROTEIN GP5*).
RX PubMed=3157805; DOI=10.1128/jvi.54.2.460-466.1985;
RA Nakagawa H., Arisaka F., Ishii S.;
RT "Isolation and characterization of the bacteriophage T4 tail-associated
RT lysozyme.";
RL J. Virol. 54:460-466(1985).
RN [8]
RP SUBCELLULAR LOCATION (BASEPLATE CENTRAL SPIKE PROTEIN GP5*), AND
RP SUBCELLULAR LOCATION (GP5C).
RX PubMed=2403438; DOI=10.1128/jvi.64.1.143-154.1990;
RA Watts N.R., Coombs D.H.;
RT "Structure of the bacteriophage T4 baseplate as determined by chemical
RT cross-linking.";
RL J. Virol. 64:143-154(1990).
RN [9]
RP REVIEW.
RX PubMed=12837775; DOI=10.1128/jb.185.14.4022-4030.2003;
RA Weigele P.R., Scanlon E., King J.;
RT "Homotrimeric, beta-stranded viral adhesins and tail proteins.";
RL J. Bacteriol. 185:4022-4030(2003).
RN [10]
RP REVIEW.
RX PubMed=14625682; DOI=10.1007/s00018-003-3072-1;
RA Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F., Rossmann M.G.;
RT "Structure and morphogenesis of bacteriophage T4.";
RL Cell. Mol. Life Sci. 60:2356-2370(2003).
RN [11]
RP FUNCTION (BASEPLATE CENTRAL SPIKE PROTEIN GP5*), AND SUBUNIT (BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5*).
RX PubMed=16956798; DOI=10.1016/j.bbapap.2006.07.007;
RA Kumar Sarkar S., Takeda Y., Kanamaru S., Arisaka F.;
RT "Association and dissociation of the cell puncturing complex of
RT bacteriophage T4 is controlled by both pH and temperature.";
RL Biochim. Biophys. Acta 1764:1487-1492(2006).
RN [12]
RP REVIEW.
RX PubMed=21129200; DOI=10.1186/1743-422x-7-355;
RA Leiman P.G., Arisaka F., van Raaij M.J., Kostyuchenko V.A., Aksyuk A.A.,
RA Kanamaru S., Rossmann M.G.;
RT "Morphogenesis of the T4 tail and tail fibers.";
RL Virol. J. 7:355-355(2010).
RN [13]
RP FUNCTION (BASEPLATE CENTRAL SPIKE PROTEIN GP5*).
RX PubMed=21793574; DOI=10.1021/ja204451g;
RA Nishima W., Kanamaru S., Arisaka F., Kitao A.;
RT "Screw motion regulates multiple functions of T4 phage protein gene product
RT 5 during cell puncturing.";
RL J. Am. Chem. Soc. 133:13571-13576(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), ACTIVE SITE, IDENTIFICATION IN A
RP COMPLEX WITH GP27; GP5C AND GP5.4 (BASEPLATE CENTRAL SPIKE PROTEIN GP5*),
RP AND IDENTIFICATION IN A COMPLEX WITH GP27; GP5* AND GP5.4 (BASEPLATE
RP CENTRAL SPIKE PROTEIN GP5C).
RX PubMed=11823865; DOI=10.1038/415553a;
RA Kanamaru S., Leiman P.G., Kostyuchenko V.A., Chipman P.R.,
RA Mesyanzhinov V.V., Arisaka F., Rossmann M.G.;
RT "Structure of the cell-puncturing device of bacteriophage T4.";
RL Nature 415:553-557(2002).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS), AND SUBCELLULAR LOCATION
RP (BASEPLATE CENTRAL SPIKE PROTEIN GP5 PRECURSOR).
RX PubMed=12923574; DOI=10.1038/nsb970;
RA Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S., van Raaij M.J.,
RA Arisaka F., Mesyanzhinov V.V., Rossmann M.G.;
RT "Three-dimensional structure of bacteriophage T4 baseplate.";
RL Nat. Struct. Biol. 10:688-693(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GP27, PROTEOLYTIC
RP CLEAVAGE (BASEPLATE CENTRAL SPIKE PROTEIN GP5 PRECURSOR), MUTAGENESIS OF
RP SER-351, AND SUBUNIT (BASEPLATE CENTRAL SPIKE PROTEIN GP5 PRECURSOR).
RX PubMed=15701513; DOI=10.1016/j.jmb.2004.12.042;
RA Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., Arisaka F.;
RT "Control of bacteriophage T4 tail lysozyme activity during the infection
RT process.";
RL J. Mol. Biol. 346:1013-1020(2005).
RN [17] {ECO:0007744|PDB:4JJ2, ECO:0007744|PDB:4OSD}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 484-575, AND SUBUNIT (GP5C).
RX PubMed=26295253; DOI=10.3390/v7082839;
RA Buth S.A., Menin L., Shneider M.M., Engel J., Boudko S.P., Leiman P.G.;
RT "Structure and Biophysical Properties of a Triple-Stranded Beta-Helix
RT Comprising the Central Spike of Bacteriophage T4.";
RL Viruses 7:4676-4706(2015).
RN [18] {ECO:0007744|PDB:5IV5}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBCELLULAR LOCATION
RP (BASEPLATE CENTRAL SPIKE PROTEIN GP5*), SUBCELLULAR LOCATION (GP5C),
RP IDENTIFICATION IN A COMPLEX WITH GP27; GP5C AND GP5.4 (BASEPLATE CENTRAL
RP SPIKE PROTEIN GP5*), AND IDENTIFICATION IN A COMPLEX WITH GP27; GP5* AND
RP GP5.4 (BASEPLATE CENTRAL SPIKE PROTEIN GP5C).
RX PubMed=27193680; DOI=10.1038/nature17971;
RA Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
RA Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
RT "Structure of the T4 baseplate and its function in triggering sheath
RT contraction.";
RL Nature 533:346-352(2016).
CC -!- FUNCTION: [Baseplate central spike protein Gp5*]: Baseplate central
CC spike complex-associated lysozyme that is essential for the localized
CC hydrolysis of bacterial cell wall, so that the tail tube, through which
CC the phage DNA is ejected, can penetrate to the host inner membrane
CC (PubMed:21129200, PubMed:21793574, PubMed:16956798, PubMed:3157805).
CC The tail lysozyme complex at the tip of the tail tube penetrates
CC through the outer membrane into the periplasm and during that process,
CC gp5* dissociates from gp5C and activated (PubMed:16956798). Due to the
CC lower pH in the periplasm, gp5* would dissociate from gp27 which
CC probably still binds to the tip of the tube (PubMed:16956798). This
CC way, lysozyme domain is released and locally digests the peptidoglycan
CC layer to make a hole to let the tube penetrate to the inner membrane
CC (PubMed:16956798). Involved in the tail assembly (PubMed:21129200).
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:16956798,
CC ECO:0000269|PubMed:21793574, ECO:0000269|PubMed:3157805,
CC ECO:0000303|PubMed:21129200}.
CC -!- CATALYTIC ACTIVITY: [Baseplate central spike protein Gp5*]:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_04151,
CC ECO:0000269|PubMed:10217762, ECO:0000269|PubMed:3157805};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [Baseplate central spike protein Gp5*]:
CC pH dependence:
CC Optimum pH is 5.8. {ECO:0000269|PubMed:3157805};
CC -!- SUBUNIT: [Baseplate central spike protein Gp5*]: Monomer
CC (PubMed:16956798). The central spike complex, which creates an
CC extension of the tail tube, is made up of three copies of the gp27-
CC gp5*-gp5C complex and one copy of gp5.4 (PubMed:11823865,
CC PubMed:27193680). Part of the baseplate macromolecular complex which
CC consists of gp5*, gp5C, gp5.4, gp27 (central spike complex); gp6, gp25,
CC gp53 (inner baseplate); gp7, gp8 (intermediate baseplate); gp9, gp10,
CC gp11, gp12 (peripheral); gp48 and gp54 (proximal region of the tail
CC tube) (PubMed:27193680). {ECO:0000255|HAMAP-Rule:MF_04151,
CC ECO:0000269|PubMed:11823865, ECO:0000269|PubMed:16956798,
CC ECO:0000269|PubMed:27193680}.
CC -!- SUBUNIT: [Gp5C]: Homotrimer (PubMed:11823865, PubMed:26295253). The
CC central spike complex, which creates an extension of the tail tube, is
CC made up of three copies of the gp27-gp5*-gp5C complex and one copy of
CC gp5.4 (PubMed:11823865, PubMed:27193680). Part of the baseplate
CC macromolecular complex which consists of gp5*, gp5C, gp5.4, gp27
CC (central spike complex); gp6, gp25, gp53 (inner baseplate); gp7, gp8
CC (intermediate baseplate); gp9, gp10, gp11, gp12 (peripheral); gp48 and
CC gp54 (proximal region of the tail tube) (PubMed:27193680).
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:11823865,
CC ECO:0000269|PubMed:26295253, ECO:0000269|PubMed:27193680}.
CC -!- SUBUNIT: [Pre-baseplate central spike protein Gp5]: Homotrimer.
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:15701513}.
CC -!- INTERACTION:
CC P16009; P17172: 27; NbExp=2; IntAct=EBI-1032754, EBI-1032762;
CC -!- SUBCELLULAR LOCATION: [Baseplate central spike protein Gp5*]: Virion
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:10217762,
CC ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438,
CC ECO:0000269|PubMed:27193680}. Note=Present in 3 copies in the
CC baseplate. {ECO:0000255|HAMAP-Rule:MF_04151,
CC ECO:0000269|PubMed:27193680}.
CC -!- SUBCELLULAR LOCATION: [Gp5C]: Virion {ECO:0000255|HAMAP-Rule:MF_04151,
CC ECO:0000269|PubMed:10217762, ECO:0000269|PubMed:15342608,
CC ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}. Note=Present
CC in 3 copies in the baseplate. {ECO:0000255|HAMAP-Rule:MF_04151,
CC ECO:0000269|PubMed:27193680}.
CC -!- SUBCELLULAR LOCATION: [Pre-baseplate central spike protein Gp5]: Virion
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:10217762,
CC ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438,
CC ECO:0000269|PubMed:27193680}. Note=Present in the baseplate.
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:12923574}.
CC -!- PTM: [Pre-baseplate central spike protein Gp5]: In the fully assembled
CC virus, gp5 precursor is cleaved to form the mature tail lysozyme gp5*,
CC and a C-terminus fragment, gp5C (PubMed:10217762, PubMed:15342608,
CC PubMed:15701513). The two fragments remain associated with the virion
CC (PubMed:10217762, PubMed:15342608). The enzymatic activity of the
CC precursor is about 10% of that of mature gp5* (PubMed:10217762).
CC PubMed:15342608 reported a cleavage at Val-390 but the cleavage has
CC been mostly observed at Ser-351 (PubMed:10217762, PubMed:15701513).
CC {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:10217762,
CC ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:15701513}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000255|HAMAP-Rule:MF_04151}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X15728; CAA33749.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42482.1; -; Genomic_DNA.
DR EMBL; X14845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S25240; G5BPT4.
DR RefSeq; NP_049757.1; NC_000866.4.
DR PDB; 1K28; X-ray; 2.90 A; A=1-575.
DR PDB; 1PDL; EM; 12.00 A; A/B/C=1-575.
DR PDB; 1WTH; X-ray; 2.80 A; A=1-575.
DR PDB; 2Z6B; X-ray; 3.11 A; A=1-575.
DR PDB; 3A1M; X-ray; 2.00 A; A/B/C/D/E/F=490-575.
DR PDB; 4JIV; X-ray; 1.90 A; A/B/C=484-575.
DR PDB; 4JIW; X-ray; 3.40 A; A/B/C/E/F/G/I/J/K/M/N/O=484-575.
DR PDB; 4JJ2; X-ray; 1.28 A; A/B/C=483-575.
DR PDB; 4KU0; X-ray; 1.15 A; A/B/C=484-575.
DR PDB; 4OSD; X-ray; 1.96 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=484-575.
DR PDB; 5IV5; EM; 4.11 A; YA/YB/YC=1-575.
DR PDB; 6P1Z; X-ray; 2.10 A; A/B/C/E/F/G=484-575.
DR PDB; 6P20; X-ray; 1.75 A; A/B/C=484-559.
DR PDB; 6P22; X-ray; 2.29 A; A/B/C=484-565.
DR PDB; 6P2A; X-ray; 1.90 A; A/B/C/D/E/F=484-561.
DR PDB; 6XC0; X-ray; 1.78 A; A/B=174-342.
DR PDB; 6XC1; X-ray; 1.92 A; A=174-342.
DR PDB; 7CN7; X-ray; 1.15 A; A=162-342.
DR PDBsum; 1K28; -.
DR PDBsum; 1PDL; -.
DR PDBsum; 1WTH; -.
DR PDBsum; 2Z6B; -.
DR PDBsum; 3A1M; -.
DR PDBsum; 4JIV; -.
DR PDBsum; 4JIW; -.
DR PDBsum; 4JJ2; -.
DR PDBsum; 4KU0; -.
DR PDBsum; 4OSD; -.
DR PDBsum; 5IV5; -.
DR PDBsum; 6P1Z; -.
DR PDBsum; 6P20; -.
DR PDBsum; 6P22; -.
DR PDBsum; 6P2A; -.
DR PDBsum; 6XC0; -.
DR PDBsum; 6XC1; -.
DR PDBsum; 7CN7; -.
DR SMR; P16009; -.
DR IntAct; P16009; 1.
DR MINT; P16009; -.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR GeneID; 1258817; -.
DR KEGG; vg:1258817; -.
DR EvolutionaryTrace; P16009; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098015; C:virus tail; IMP:CAFA.
DR GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:CAFA.
DR GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
DR GO; GO:0044409; P:entry into host; IDA:UniProtKB.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IMP:CAFA.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.40; -; 1.
DR HAMAP; MF_04151; NEEDLE_T4; 1.
DR InterPro; IPR002196; Glyco_hydro_24.
DR InterPro; IPR010609; Gp5_C.
DR InterPro; IPR009590; Gp5_OB_N.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR InterPro; IPR046397; NEEDLE_T4.
DR InterPro; IPR001165; T4-type_lysozyme.
DR Pfam; PF06715; Gp5_C; 3.
DR Pfam; PF06714; Gp5_OB; 1.
DR Pfam; PF00959; Phage_lysozyme; 1.
DR PRINTS; PR00684; T4LYSOZYME.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry;
KW Direct protein sequencing; Glycosidase; Hydrolase; Late protein;
KW Reference proteome; Viral baseplate protein;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Viral tail assembly; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..575
FT /note="Pre-baseplate central spike protein Gp5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04151"
FT /id="PRO_0000218111"
FT CHAIN 1..351
FT /note="Baseplate central spike protein Gp5*"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04151"
FT /id="PRO_0000408360"
FT CHAIN 352..575
FT /note="Gp5C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04151"
FT /id="PRO_0000408361"
FT REGION 150..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04151,
FT ECO:0000305|PubMed:11823865"
FT ACT_SITE 193
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04151,
FT ECO:0000305|PubMed:11823865"
FT SITE 351..352
FT /note="Cleavage"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04151,
FT ECO:0000269|PubMed:10217762, ECO:0000269|PubMed:15701513"
FT MUTAGEN 351
FT /note="S->A,H: Reduced proteolytic cleavage of the pre-
FT baseplate central spike protein Gp5."
FT /evidence="ECO:0000269|PubMed:15701513"
FT MUTAGEN 351
FT /note="S->K,Q,T,Y: Complete loss of proteolytic cleavage of
FT the Pre-baseplate central spike protein Gp5."
FT /evidence="ECO:0000269|PubMed:15701513"
FT MUTAGEN 351
FT /note="S->L: Complete loss of proteolytic cleavage of the
FT Pre-baseplate central spike protein Gp5. 90% loss of
FT lysozyme activity."
FT /evidence="ECO:0000269|PubMed:15701513"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1WTH"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1WTH"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2Z6B"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:1WTH"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1WTH"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:1WTH"
FT HELIX 143..149
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1WTH"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1WTH"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:7CN7"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:7CN7"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1K28"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:7CN7"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 214..225
FT /evidence="ECO:0007829|PDB:7CN7"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 238..258
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 293..300
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:7CN7"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:7CN7"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:6XC0"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:7CN7"
FT STRAND 347..350
FT /evidence="ECO:0007829|PDB:1WTH"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:1WTH"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 510..516
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 518..524
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 526..532
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 542..563
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:4KU0"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:4KU0"
SQ SEQUENCE 575 AA; 63116 MW; 6CC2D04E05155CF5 CRC64;
MEMISNNLNW FVGVVEDRMD PLKLGRVRVR VVGLHPPQRA QGDVMGIPTE KLPWMSVIQP
ITSAAMSGIG GSVTGPVEGT RVYGHFLDKW KTNGIVLGTY GGIVREKPNR LEGFSDPTGQ
YPRRLGNDTN VLNQGGEVGY DSSSNVIQDS NLDTAINPDD RPLSEIPTDD NPNMSMAEML
RRDEGLRLKV YWDTEGYPTI GIGHLIMKQP VRDMAQINKV LSKQVGREIT GNPGSITMEE
ATTLFERDLA DMQRDIKSHS KVGPVWQAVN RSRQMALENM AFQMGVGGVA KFNTMLTAML
AGDWEKAYKA GRDSLWYQQT KGRASRVTMI ILTGNLESYG VEVKTPARSL SAMAATVAKS
SDPADPPIPN DSRILFKEPV SSYKGEYPYV HTMETESGHI QEFDDTPGQE RYRLVHPTGT
YEEVSPSGRR TRKTVDNLYD ITNADGNFLV AGDKKTNVGG SEIYYNMDNR LHQIDGSNTI
FVRGDETKTV EGNGTILVKG NVTIIVEGNA DITVKGDATT LVEGNQTNTV NGNLSWKVAG
TVDWDVGGDW TEKMASMSSI SSGQYTIDGS RIDIG
