EXLYS_BPT7
ID EXLYS_BPT7 Reviewed; 1318 AA.
AC P03726;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Peptidoglycan transglycosylase gp16 {ECO:0000255|HAMAP-Rule:MF_04121};
DE EC=4.2.2.n1 {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:14763988};
DE AltName: Full=Internal core protein gp16 {ECO:0000255|HAMAP-Rule:MF_04121};
GN OrderedLocusNames=16;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP DOMAIN.
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 [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10926491; DOI=10.1006/jmbi.2000.3940;
RA Struthers-Schlinke J.S., Robins W.P., Kemp P., Molineux I.J.;
RT "The internal head protein Gp16 controls DNA ejection from the
RT bacteriophage T7 virion.";
RL J. Mol. Biol. 301:35-45(2000).
RN [4]
RP FUNCTION, AND DOMAIN.
RX PubMed=14763988; DOI=10.1046/j.1365-2958.2003.03894.x;
RA Moak M., Molineux I.J.;
RT "Peptidoglycan hydrolytic activities associated with bacteriophage
RT virions.";
RL Mol. Microbiol. 51:1169-1183(2004).
RN [5]
RP FUNCTION.
RX PubMed=20036409; DOI=10.1016/j.virol.2009.12.002;
RA Chang C.Y., Kemp P., Molineux I.J.;
RT "Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the
RT infected cell.";
RL Virology 398:176-186(2010).
RN [6]
RP INTERACTION WITH GP15, AND SUBUNIT.
RX PubMed=23580619; DOI=10.1073/pnas.1215563110;
RA Guo F., Liu Z., Vago F., Ren Y., Wu W., Wright E.T., Serwer P., Jiang W.;
RT "Visualization of uncorrelated, tandem symmetry mismatches in the internal
RT genome packaging apparatus of bacteriophage T7.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6811-6816(2013).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=23306440; DOI=10.1126/science.1231887;
RA Hu B., Margolin W., Molineux I.J., Liu J.;
RT "The bacteriophage t7 virion undergoes extensive structural remodeling
RT during infection.";
RL Science 339:576-579(2013).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=23884409; DOI=10.1074/jbc.m113.491209;
RA Cuervo A., Pulido-Cid M., Chagoyen M., Arranz R., Gonzalez-Garcia V.A.,
RA Garcia-Doval C., Caston J.R., Valpuesta J.M., van Raaij M.J.,
RA Martin-Benito J., Carrascosa J.L.;
RT "Structural characterization of the bacteriophage T7 tail machinery.";
RL J. Biol. Chem. 288:26290-26299(2013).
RN [9]
RP REVIEW.
RX PubMed=22991936; DOI=10.3109/1040841x.2012.723675;
RA Rodriguez-Rubio L., Martinez B., Donovan D.M., Rodriguez A., Garcia P.;
RT "Bacteriophage virion-associated peptidoglycan hydrolases: potential new
RT enzybiotics.";
RL Crit. Rev. Microbiol. 39:427-434(2013).
RN [10]
RP INTERACTION WITH GP15, FUNCTION, AND TOPOLOGY.
RX PubMed=26476287; DOI=10.1016/j.virol.2015.09.022;
RA Lupo D., Leptihn S., Nagler G., Haase M., Molineux I.J., Kuhn A.;
RT "The T7 ejection nanomachine components gp15-gp16 form a spiral ring
RT complex that binds DNA and a lipid membrane.";
RL Virology 486:263-271(2015).
CC -!- FUNCTION: Component of the cylindrical core that assembles on the inner
CC surface of the capsid during capsid formation and plays a role in viral
CC DNA ejection into the host cell. The inner core is composed of stacked
CC rings of gp14, gp15 and gp16 proteins. Following binding to the host
CC cell surface, the internal core is diassembled and gp16 is ejected
CC along with gp14 and gp15 into the infected cell. Gp16 probably inserts
CC in the host inner membrane and remains associated with gp15. The gp15-
CC gp16 complex binds to both the viral DNA and the host inner membrane,
CC probably escorting the leading end of the genome through the periplasm
CC and controlling the extend of DNA translocated into the host cell.
CC Functions as an exolysin that catalyzes the cleavage of the glycosidic
CC bonds between N-acetylmuramic acid and N-acetylglucosamine residues in
CC peptidoglycans allowing the local digestion of the bacterial
CC peptidoglycan wall. {ECO:0000255|HAMAP-Rule:MF_04121,
CC ECO:0000269|PubMed:10926491, ECO:0000269|PubMed:14763988,
CC ECO:0000269|PubMed:20036409, ECO:0000269|PubMed:26476287}.
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:0000255|HAMAP-Rule:MF_04121,
CC ECO:0000269|PubMed:14763988};
CC -!- SUBUNIT: Homotetramer. Interacts with gp15; after ejection the gp15-
CC gp16 complex composed of a gp15 octamer and a gp16 tetramer probably
CC binds both the viral DNA and the host inner membrane.
CC {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23580619,
CC ECO:0000269|PubMed:26476287}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04121,
CC ECO:0000269|PubMed:23884409}. Host cell inner membrane
CC {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23306440}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04121}. Note=The gp15-
CC gp16 complex spans the periplasm and the cytoplasmic membrane.
CC {ECO:0000255|HAMAP-Rule:MF_04121, ECO:0000269|PubMed:23306440}.
CC -!- DOMAIN: The N-terminus contains the transglycosylase activity
CC (Potential). The C-terminus is essential for the viral DNA
CC translocation into the host cytoplasm. {ECO:0000255|HAMAP-
CC Rule:MF_04121, ECO:0000269|PubMed:20036409}.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000255|HAMAP-Rule:MF_04121}.
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DR EMBL; V01146; CAA24434.1; -; Genomic_DNA.
DR PIR; A04352; HIBPD7.
DR RefSeq; NP_042004.1; NC_001604.1.
DR PDB; 6YT5; EM; 3.00 A; G/H/I/J/K/L=1-1318.
DR PDB; 7EYB; EM; 3.70 A; I/J/K/L=1-1318.
DR PDB; 7K5C; EM; 2.70 A; B/D/F/G/J/L=1-1318.
DR PDBsum; 6YT5; -.
DR PDBsum; 7EYB; -.
DR PDBsum; 7K5C; -.
DR SMR; P03726; -.
DR IntAct; P03726; 1.
DR MINT; P03726; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR TCDB; 3.A.17.1.1; the phage t7 injectisome (t7 injectisome) family.
DR GeneID; 1261031; -.
DR KEGG; vg:1261031; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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:0044409; P:entry into host; IDA:UniProtKB.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR GO; GO:0039678; P:viral genome ejection through host cell envelope; IMP:UniProtKB.
DR GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW.
DR HAMAP; MF_04121; TRANSGLYCOSYLASE_T7; 1.
DR InterPro; IPR038994; Gp16.
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 3D-structure; Antimicrobial; Bacteriolytic enzyme;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry;
KW Host cell inner membrane; Host cell membrane; Host membrane; Hydrolase;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral short tail ejection system;
KW Virion; Virus entry into host cell.
FT CHAIN 1..1318
FT /note="Peptidoglycan transglycosylase gp16"
FT /id="PRO_0000196560"
FT TOPO_DOM 1..1136
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04121,
FT ECO:0000305|PubMed:26476287"
FT TRANSMEM 1137..1157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04121"
FT TOPO_DOM 1158..1318
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04121,
FT ECO:0000305|PubMed:26476287"
FT REGION 24..111
FT /note="Transglycosylase SLT-type domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04121"
FT REGION 1314..1318
FT /note="Essential for viral DNA translocation"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04121,
FT ECO:0000269|PubMed:20036409"
FT ACT_SITE 37
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04121"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 79..95
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 133..140
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:7K5C"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:7K5C"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:7K5C"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:7K5C"
SQ SEQUENCE 1318 AA; 143838 MW; 51A0AAA920CBF210 CRC64;
MDKYDKNVPS DYDGLFQKAA DANGVSYDLL RKVAWTESRF VPTAKSKTGP LGMMQFTKAT
AKALGLRVTD GPDDDRLNPE LAINAAAKQL AGLVGKFDGD ELKAALAYNQ GEGRLGNPQL
EAYSKGDFAS ISEEGRNYMR NLLDVAKSPM AGQLETFGGI TPKGKGIPAE VGLAGIGHKQ
KVTQELPEST SFDVKGIEQE ATAKPFAKDF WETHGETLDE YNSRSTFFGF KNAAEAELSN
SVAGMAFRAG RLDNGFDVFK DTITPTRWNS HIWTPEELEK IRTEVKNPAY INVVTGGSPE
NLDDLIKLAN ENFENDSRAA EAGLGAKLSA GIIGAGVDPL SYVPMVGVTG KGFKLINKAL
VVGAESAALN VASEGLRTSV AGGDADYAGA ALGGFVFGAG MSAISDAVAA GLKRSKPEAE
FDNEFIGPMM RLEARETARN ANSADLSRMN TENMKFEGEH NGVPYEDLPT ERGAVVLHDG
SVLSASNPIN PKTLKEFSEV DPEKAARGIK LAGFTEIGLK TLGSDDADIR RVAIDLVRSP
TGMQSGASGK FGATASDIHE RLHGTDQRTY NDLYKAMSDA MKDPEFSTGG AKMSREETRY
TIYRRAALAI ERPELQKALT PSERIVMDII KRHFDTKREL MENPAIFGNT KAVSIFPESR
HKGTYVPHVY DRHAKALMIQ RYGAEGLQEG IARSWMNSYV SRPEVKARVD EMLKELHGVK
EVTPEMVEKY AMDKAYGISH SDQFTNSSII EENIEGLVGI ENNSFLEARN LFDSDLSITM
PDGQQFSVND LRDFDMFRIM PAYDRRVNGD IAIMGSTGKT TKELKDEILA LKAKAEGDGK
KTGEVHALMD TVKILTGRAR RNQDTVWETS LRAINDLGFF AKNAYMGAQN ITEIAGMIVT
GNVRALGHGI PILRDTLYKS KPVSAKELKE LHASLFGKEV DQLIRPKRAD IVQRLREATD
TGPAVANIVG TLKYSTQELA ARSPWTKLLN GTTNYLLDAA RQGMLGDVIS ATLTGKTTRW
EKEGFLRGAS VTPEQMAGIK SLIKEHMVRG EDGKFTVKDK QAFSMDPRAM DLWRLADKVA
DEAMLRPHKV SLQDSHAFGA LGKMVMQFKS FTIKSLNSKF LRTFYDGYKN NRAIDAALSI
ITSMGLAGGF YAMAAHVKAY ALPKEKRKEY LERALDPTMI AHAALSRSSQ LGAPLAMVDL
VGGVLGFESS KMARSTILPK DTVKERDPNK PYTSREVMGA MGSNLLEQMP SAGFVANVGA
TLMNAAGVVN SPNKATEQDF MTGLMNSTKE LVPNDPLTQQ LVLKIYEANG VNLRERRK
