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 24-JAN-2024, entry version 154. 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 Straboviridae; 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 OrthoDB; 2186at10239; -. DR EvolutionaryTrace; P16009; -. DR Proteomes; UP000009087; Segment. 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: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-UniRule. DR GO; GO:0098994; P:disruption of host cell envelope during viral entry; IEA:UniProtKB-KW. DR GO; GO:0044409; P:entry into host; IDA:UniProtKB. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0046718; P:viral entry into host cell; IMP:CAFA. DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-UniRule. DR CDD; cd00735; T4-like_lys; 1. DR Gene3D; 1.10.530.40; -; 1. DR Gene3D; 3.10.450.190; -; 1. DR Gene3D; 2.40.50.260; Nucleic acid-binding protein domain; 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 PANTHER; PTHR37406; T4-TYPE LYSOZYME 1-RELATED; 1. DR PANTHER; PTHR37406:SF1; T4-TYPE LYSOZYME 1-RELATED; 1. DR Pfam; PF06715; Gp5_C; 3. DR Pfam; PF06714; Gp5_OB; 1. DR Pfam; PF00959; Phage_lysozyme; 1. DR PRINTS; PR00684; T4LYSOZYME. DR SUPFAM; SSF69255; gp5 N-terminal domain-like; 1. DR SUPFAM; SSF53955; Lysozyme-like; 1. DR SUPFAM; SSF69349; Phage fibre proteins; 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 FT pre-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 //