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Baseplate central spike complex protein gp5 (Peptidoglycan hydrolase gp5) (EC 3.2.1.17) (Protein Gp5) [Cleaved into: Gp5*; Gp5C]

 BP5_BPT4                Reviewed;         575 AA.
P16009;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 2.
22-NOV-2017, entry version 127.
RecName: Full=Baseplate central spike complex protein gp5 {ECO:0000303|PubMed:27193680};
AltName: Full=Peptidoglycan hydrolase gp5;
EC=3.2.1.17 {ECO:0000269|PubMed:3157805};
AltName: Full=Protein Gp5;
Contains:
RecName: Full=Gp5*;
Contains:
RecName: Full=Gp5C;
Name=5;
Enterobacteria phage T4 (Bacteriophage T4).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Myoviridae;
Tevenvirinae; T4virus.
NCBI_TaxID=10665;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2488704;
Mosig G., Lin G.W., Franklin J., Fan W.H.;
"Functional relationships and structural determinants of two
bacteriophage T4 lysozymes: a soluble (gene e) and a baseplate-
associated (gene 5) protein.";
New Biol. 1:171-179(1989).
[2]
SEQUENCE REVISION.
Mosig G.;
Submitted (MAR-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12626685; DOI=10.1128/MMBR.67.1.86-156.2003;
Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
"Bacteriophage T4 genome.";
Microbiol. Mol. Biol. Rev. 67:86-156(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
PubMed=2740234; DOI=10.1093/nar/17.11.4392;
Koch T., Lamm N., Rueger W.;
"Sequencing, cloning and overexpression of genes of bacteriophage T4
between map positions 74.325 and 77.184.";
Nucleic Acids Res. 17:4392-4392(1989).
[5]
IDENTIFICATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC
ACTIVITY.
PubMed=3157805;
Nakagawa H., Arisaka F., Ishii S.;
"Isolation and characterization of the bacteriophage T4 tail-
associated lysozyme.";
J. Virol. 54:460-466(1985).
[6]
SUBCELLULAR LOCATION.
PubMed=2403438;
Watts N.R., Coombs D.H.;
"Structure of the bacteriophage T4 baseplate as determined by chemical
cross-linking.";
J. Virol. 64:143-154(1990).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GP27, SUBUNIT, AND
PROTEOLYTIC CLEAVAGE.
PubMed=12837775; DOI=10.1128/JB.185.14.4022-4030.2003;
Weigele P.R., Scanlon E., King J.;
"Homotrimeric, beta-stranded viral adhesins and tail proteins.";
J. Bacteriol. 185:4022-4030(2003).
[8]
REVIEW.
PubMed=14625682; DOI=10.1007/s00018-003-3072-1;
Leiman P.G., Kanamaru S., Mesyanzhinov V.V., Arisaka F.,
Rossmann M.G.;
"Structure and morphogenesis of bacteriophage T4.";
Cell. Mol. Life Sci. 60:2356-2370(2003).
[9]
REVIEW ON FUNCTION.
PubMed=21129200; DOI=10.1186/1743-422X-7-355;
Leiman P.G., Arisaka F., van Raaij M.J., Kostyuchenko V.A.,
Aksyuk A.A., Kanamaru S., Rossmann M.G.;
"Morphogenesis of the T4 tail and tail fibers.";
Virol. J. 7:355-355(2010).
[10]
SUBUNIT.
PubMed=19896486; DOI=10.1016/j.jmb.2009.10.071;
Yap M.L., Mio K., Leiman P.G., Kanamaru S., Arisaka F.;
"The baseplate wedges of bacteriophage T4 spontaneously assemble into
hubless baseplate-like structure in vitro.";
J. Mol. Biol. 395:349-360(2010).
[11]
STRUCTURE BY ELECTRON MICROSCOPY (12.0 ANGSTROMS).
PubMed=12923574; DOI=10.1038/nsb970;
Kostyuchenko V.A., Leiman P.G., Chipman P.R., Kanamaru S.,
van Raaij M.J., Arisaka F., Mesyanzhinov V.V., Rossmann M.G.;
"Three-dimensional structure of bacteriophage T4 baseplate.";
Nat. Struct. Biol. 10:688-693(2003).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=11823865; DOI=10.1038/415553a;
Kanamaru S., Leiman P.G., Kostyuchenko V.A., Chipman P.R.,
Mesyanzhinov V.V., Arisaka F., Rossmann M.G.;
"Structure of the cell-puncturing device of bacteriophage T4.";
Nature 415:553-557(2002).
[13]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=15701513; DOI=10.1016/j.jmb.2004.12.042;
Kanamaru S., Ishiwata Y., Suzuki T., Rossmann M.G., Arisaka F.;
"Control of bacteriophage T4 tail lysozyme activity during the
infection process.";
J. Mol. Biol. 346:1013-1020(2005).
[14] {ECO:0000244|PDB:5IV5}
STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT,
SUBCELLULAR LOCATION, INTERACTION WITH GP27, AND INTERACTION WITH
GP5.4.
PubMed=27193680; DOI=10.1038/nature17971;
Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
"Structure of the T4 baseplate and its function in triggering sheath
contraction.";
Nature 533:346-352(2016).
-!- FUNCTION: Baseplate central spike complex-associated lysozyme that
is essential for the localized hydrolysis of bacterial cell wall
in the periplasmic space, a necessary step for viral DNA ejection
into the host cell. Involved in the tail assembly.
{ECO:0000269|PubMed:12837775, ECO:0000303|PubMed:21129200}.
-!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-beta-linkages between N-
acetylmuramic acid and N-acetyl-D-glucosamine residues in a
peptidoglycan and between N-acetyl-D-glucosamine residues in
chitodextrins. {ECO:0000269|PubMed:3157805}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.8. {ECO:0000269|PubMed:3157805};
-!- SUBUNIT: Homotrimer (PubMed:12837775, PubMed:19896486,
PubMed:11823865). Heteromultimer with gp27 trimer and gp5.4
monomer; this interaction forms the central spike complex that
creates an extension of the tail tube (PubMed:12837775,
PubMed:27193680). The central spike complex is made up of three
copies of the gp27-gp5*-gp5C complex and one copy of gp5.4
(PubMed:11823865, PubMed:27193680). Part of the baseplate
macromolecular complex which consists of gp5, gp5.4, gp27 (central
spike complex); gp6, gp25, gp53 (inner baseplate); gp7, gp8
(intermediate baseplate); gp9, gp10, gp11, gp12 (peripheral); gp48
and gp54 (proximal region of the tail tube) (PubMed:27193680).
{ECO:0000269|PubMed:11823865, ECO:0000269|PubMed:12837775,
ECO:0000269|PubMed:19896486, ECO:0000269|PubMed:27193680,
ECO:0000303|PubMed:21129200}.
-!- INTERACTION:
P17172:27; NbExp=2; IntAct=EBI-1032754, EBI-1032762;
-!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:12837775,
ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}.
Note=Present in 3 copies in the baseplate.
{ECO:0000269|PubMed:27193680, ECO:0000303|PubMed:21129200}.
-!- PTM: In the fully assembled virus, gp5 is cleaved after residue
351, but the resulting fragments, gp5* and gp5C, remain associated
with the virion. {ECO:0000269|PubMed:12837775}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X15728; CAA33749.1; -; Genomic_DNA.
EMBL; AF158101; AAD42482.1; -; Genomic_DNA.
EMBL; X14845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; S25240; G5BPT4.
RefSeq; NP_049757.1; NC_000866.4.
PDB; 1K28; X-ray; 2.90 A; A=1-575.
PDB; 1PDL; EM; 12.00 A; A/B/C=1-575.
PDB; 1WTH; X-ray; 2.80 A; A=1-575.
PDB; 2Z6B; X-ray; 3.11 A; A=1-575.
PDB; 3A1M; X-ray; 2.00 A; A/B/C/D/E/F=490-575.
PDB; 4JIV; X-ray; 1.90 A; A/B/C=484-575.
PDB; 4JIW; X-ray; 3.40 A; A/B/C/E/F/G/I/J/K/M/N/O=484-575.
PDB; 4JJ2; X-ray; 1.28 A; A/B/C=483-575.
PDB; 4KU0; X-ray; 1.15 A; A/B/C=484-575.
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.
PDB; 5IV5; EM; 4.11 A; YA/YB/YC=1-575.
PDBsum; 1K28; -.
PDBsum; 1PDL; -.
PDBsum; 1WTH; -.
PDBsum; 2Z6B; -.
PDBsum; 3A1M; -.
PDBsum; 4JIV; -.
PDBsum; 4JIW; -.
PDBsum; 4JJ2; -.
PDBsum; 4KU0; -.
PDBsum; 4OSD; -.
PDBsum; 5IV5; -.
DisProt; DP00284; -.
ProteinModelPortal; P16009; -.
SMR; P16009; -.
IntAct; P16009; 1.
MINT; MINT-231912; -.
CAZy; GH24; Glycoside Hydrolase Family 24.
TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
GeneID; 1258817; -.
KEGG; vg:1258817; -.
OrthoDB; VOG0900001V; -.
EvolutionaryTrace; P16009; -.
Proteomes; UP000009087; Genome.
GO; GO:0019012; C:virion; IDA:CACAO.
GO; GO:0098015; C:virus tail; IMP:CAFA.
GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IMP:CAFA.
GO; GO:0003796; F:lysozyme activity; IDA:UniProtKB.
GO; GO:0033922; F:peptidoglycan beta-N-acetylmuramidase activity; IDA:CACAO.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
GO; GO:0085027; P:entry into host via enzymatic degradation of host anatomical structure; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IMP:CAFA.
GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
GO; GO:0070207; P:protein homotrimerization; IMP:CAFA.
GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
Gene3D; 1.10.530.40; -; 1.
InterPro; IPR002196; Glyco_hydro_24.
InterPro; IPR010609; Gp5_C.
InterPro; IPR009590; Gp5_OB_N.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR023347; Lysozyme_dom_sf.
InterPro; IPR001165; T4-type_lysozyme.
Pfam; PF06715; Gp5_C; 3.
Pfam; PF06714; Gp5_OB; 1.
Pfam; PF00959; Phage_lysozyme; 1.
PRINTS; PR00684; T4LYSOZYME.
SUPFAM; SSF53955; SSF53955; 1.
1: Evidence at protein level;
3D-structure; Antimicrobial; Bacteriolytic enzyme; Complete proteome;
Degradation of host cell envelope components during virus entry;
Degradation of host peptidoglycans during virus entry; Glycosidase;
Hydrolase; Late protein; Reference proteome; Viral baseplate protein;
Viral genome ejection through host cell envelope;
Viral penetration into host cytoplasm; Viral release from host cell;
Viral tail assembly; Viral tail protein; Virion;
Virus entry into host cell.
CHAIN 1 575 Baseplate central spike complex protein
gp5.
/FTId=PRO_0000218111.
CHAIN 1 351 Gp5*. {ECO:0000269|PubMed:12837775}.
/FTId=PRO_0000408360.
CHAIN 352 575 Gp5C. {ECO:0000269|PubMed:12837775}.
/FTId=PRO_0000408361.
ACT_SITE 184 184 Proton donor. {ECO:0000250}.
ACT_SITE 193 193 Nucleophile. {ECO:0000250}.
SITE 351 352 Cleavage.
STRAND 9 17 {ECO:0000244|PDB:1WTH}.
STRAND 27 31 {ECO:0000244|PDB:1WTH}.
TURN 32 34 {ECO:0000244|PDB:1WTH}.
STRAND 43 45 {ECO:0000244|PDB:1WTH}.
HELIX 49 51 {ECO:0000244|PDB:1WTH}.
STRAND 54 57 {ECO:0000244|PDB:1WTH}.
STRAND 69 71 {ECO:0000244|PDB:1WTH}.
STRAND 81 86 {ECO:0000244|PDB:1WTH}.
STRAND 94 99 {ECO:0000244|PDB:1WTH}.
STRAND 103 106 {ECO:0000244|PDB:1WTH}.
STRAND 112 115 {ECO:0000244|PDB:1WTH}.
STRAND 117 119 {ECO:0000244|PDB:2Z6B}.
STRAND 124 129 {ECO:0000244|PDB:1WTH}.
HELIX 131 134 {ECO:0000244|PDB:1WTH}.
HELIX 136 140 {ECO:0000244|PDB:1WTH}.
HELIX 143 149 {ECO:0000244|PDB:1WTH}.
STRAND 154 156 {ECO:0000244|PDB:1WTH}.
TURN 163 165 {ECO:0000244|PDB:1WTH}.
HELIX 176 184 {ECO:0000244|PDB:1WTH}.
STRAND 187 192 {ECO:0000244|PDB:1WTH}.
STRAND 194 196 {ECO:0000244|PDB:1K28}.
STRAND 198 201 {ECO:0000244|PDB:1WTH}.
STRAND 204 206 {ECO:0000244|PDB:1WTH}.
HELIX 214 225 {ECO:0000244|PDB:1WTH}.
TURN 231 234 {ECO:0000244|PDB:1WTH}.
HELIX 238 257 {ECO:0000244|PDB:1WTH}.
HELIX 262 268 {ECO:0000244|PDB:1WTH}.
HELIX 271 284 {ECO:0000244|PDB:1WTH}.
HELIX 286 290 {ECO:0000244|PDB:1WTH}.
HELIX 293 300 {ECO:0000244|PDB:1WTH}.
HELIX 304 311 {ECO:0000244|PDB:1WTH}.
HELIX 315 318 {ECO:0000244|PDB:1WTH}.
TURN 319 322 {ECO:0000244|PDB:1WTH}.
HELIX 323 333 {ECO:0000244|PDB:1WTH}.
STRAND 334 336 {ECO:0000244|PDB:1WTH}.
HELIX 337 339 {ECO:0000244|PDB:1WTH}.
STRAND 347 350 {ECO:0000244|PDB:1WTH}.
TURN 354 356 {ECO:0000244|PDB:1WTH}.
STRAND 373 377 {ECO:0000244|PDB:1WTH}.
STRAND 389 394 {ECO:0000244|PDB:1WTH}.
STRAND 400 404 {ECO:0000244|PDB:1WTH}.
STRAND 411 415 {ECO:0000244|PDB:1WTH}.
STRAND 421 424 {ECO:0000244|PDB:1WTH}.
STRAND 430 433 {ECO:0000244|PDB:1WTH}.
STRAND 486 492 {ECO:0000244|PDB:4KU0}.
STRAND 494 500 {ECO:0000244|PDB:4KU0}.
STRAND 502 508 {ECO:0000244|PDB:4KU0}.
STRAND 510 516 {ECO:0000244|PDB:4KU0}.
STRAND 518 524 {ECO:0000244|PDB:4KU0}.
STRAND 526 532 {ECO:0000244|PDB:4KU0}.
STRAND 534 540 {ECO:0000244|PDB:4KU0}.
STRAND 542 563 {ECO:0000244|PDB:4KU0}.
STRAND 565 568 {ECO:0000244|PDB:4KU0}.
STRAND 570 574 {ECO:0000244|PDB:4KU0}.
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


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