EXLYS_BPPRD
ID EXLYS_BPPRD Reviewed; 265 AA.
AC P27380; Q3T4M0; Q3T4M1;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 23-FEB-2022, entry version 107.
DE RecName: Full=Transglycosylase;
DE EC=4.2.2.n1 {ECO:0000269|PubMed:10931330};
DE AltName: Full=Protein P7;
GN Name=VII;
OS Enterobacteria phage PRD1 (Bacteriophage PRD1).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Kalamavirales; Tectiviridae; Alphatectivirus.
OX NCBI_TaxID=10658;
OH NCBI_TaxID=471; Acinetobacter calcoaceticus.
OH NCBI_TaxID=562; Escherichia coli.
OH NCBI_TaxID=584; Proteus mirabilis.
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
OH NCBI_TaxID=294; Pseudomonas fluorescens.
OH NCBI_TaxID=303; Pseudomonas putida (Arthrobacter siderocapsulatus).
OH NCBI_TaxID=90371; Salmonella typhimurium.
OH NCBI_TaxID=666; Vibrio cholerae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1853567; DOI=10.1016/0042-6822(91)90995-n;
RA Bamford J.K.H., Haenninen A.-L., Pakula T.M., Ojala P.M., Kalkkinen N.,
RA Frilander M., Bamford D.H.;
RT "Genome organization of membrane-containing bacteriophage PRD1.";
RL Virology 183:658-676(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15946683; DOI=10.1016/j.jmb.2005.04.059;
RA Saren A.M., Ravantti J.J., Benson S.D., Burnett R.M., Paulin L.,
RA Bamford D.H., Bamford J.K.H.;
RT "A snapshot of viral evolution from genome analysis of the tectiviridae
RT family.";
RL J. Mol. Biol. 350:427-440(2005).
RN [3]
RP SIMILARITY TO SLT.
RX PubMed=8203016; DOI=10.1016/0968-0004(94)90201-1;
RA Koonin E.V., Rudd K.E.;
RT "A conserved domain in putative bacterial and bacteriophage
RT transglycosylases.";
RL Trends Biochem. Sci. 19:106-107(1994).
RN [4]
RP ALTERNATIVE INITIATION, AND CATALYTIC ACTIVITY.
RX PubMed=10931330; DOI=10.1046/j.1365-2958.2000.01996.x;
RA Rydman P.S., Bamford D.H.;
RT "Bacteriophage PRD1 DNA entry uses a viral membrane-associated
RT transglycosylase activity.";
RL Mol. Microbiol. 37:356-363(2000).
RN [5]
RP SUBCELLULAR LOCATION (P7), AND SUBCELLULAR LOCATION (P14).
RX PubMed=11741849; DOI=10.1128/jb.184.1.104-110.2002;
RA Rydman P.S., Bamford D.H.;
RT "The lytic enzyme of bacteriophage PRD1 is associated with the viral
RT membrane.";
RL J. Bacteriol. 184:104-110(2002).
RN [6]
RP FUNCTION (ISOFORM P7).
RX PubMed=12453208; DOI=10.1046/j.1365-2958.2002.03250.x;
RA Grahn A.M., Daugelavicius R., Bamford D.H.;
RT "Sequential model of phage PRD1 DNA delivery: active involvement of the
RT viral membrane.";
RL Mol. Microbiol. 46:1199-1209(2002).
CC -!- FUNCTION: [Isoform Transglycosylase P7]: Component of the phage
CC ejection machinery which acts as an exolysin. Muralytic protein
CC involved in host peptidoglycan digestion necessary for viral DNA entry
CC into the host cell. {ECO:0000269|PubMed:12453208}.
CC -!- FUNCTION: [Isoform Protein P14]: Does not display any enzymatic
CC activity. Required for DNA injection in the membrane transformation
CC event. Involved in the formation of the membrane tail tube to connect
CC the virus interior with the host cytosol. Essential for viral
CC infectivity. {ECO:0000269|PubMed:12453208}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC Evidence={ECO:0000269|PubMed:10931330};
CC -!- SUBUNIT: Heteromultimer composed of proteins P7 and P14. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform Transglycosylase P7]: Virion membrane
CC {ECO:0000269|PubMed:11741849}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11741849}. Note=Part of the capsid inner membrane.
CC Approximately 20 copies per virion. {ECO:0000303|PubMed:10931330}.
CC -!- SUBCELLULAR LOCATION: [Isoform Protein P14]: Virion membrane
CC {ECO:0000269|PubMed:11741849}; Single-pass membrane protein
CC {ECO:0000305}. Note=Approximately 20 copies per virion.
CC {ECO:0000303|PubMed:10931330}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Transglycosylase P7 {ECO:0000269|PubMed:10931330};
CC IsoId=P27380-1; Sequence=Displayed;
CC Name=Protein P14 {ECO:0000269|PubMed:10931330};
CC IsoId=P27380-2; Sequence=VSP_022588;
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
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DR EMBL; AY848689; AAX45907.1; -; Genomic_DNA.
DR EMBL; AY848689; AAX45925.1; -; Genomic_DNA.
DR PIR; B36777; WMBPG7.
DR RefSeq; NP_040700.1; NC_001421.2.
DR RefSeq; YP_001542614.1; NC_001421.2.
DR SMR; P27380; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR Proteomes; UP000002143; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0039641; C:viral inner membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IDA:CACAO.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003796; F:lysozyme activity; IDA:CACAO.
DR GO; GO:0008933; F:lytic transglycosylase activity; 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:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Antimicrobial; Bacteriolytic enzyme;
KW Capsid inner membrane protein;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry;
KW Direct protein sequencing; Lyase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT CHAIN 2..265
FT /note="Transglycosylase"
FT /id="PRO_0000196561"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 19..98
FT /note="Slt-type domain"
FT ACT_SITE 32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10071"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform Protein P14)"
FT /evidence="ECO:0000305"
FT /id="VSP_022588"
SQ SEQUENCE 265 AA; 27074 MW; 332B210FC6136F3C CRC64;
MSGALQWWET IGAASAQYNL DPRLVAGVVQ TESSGNPRTT SGVGAMGLMQ LMPATAKSLG
VTNAYDPTQN IYGGAALLRE NLDRYGDVNT ALLAYHGGTN QANWGAKTKS YPGKVMKNIN
LLFGNSGPVV TPAAGIAPVS GAQEMTAVNI SDYTAPDLTG LTMGAGSPDF TGGASGSWGE
ENIPWYRVDK HVANAAGSAY DAVTDAVSAP VEAAGNYALR GVVIIAAVAI VVVGLYFLFQ
DEINSAAMKM IPAGKAAGAA AKALA
