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Terminase, large subunit (EC 3.1.-.-) (DNA-packaging protein Gp17) (Gene product 17) (gp17)

 TERL_BPT4               Reviewed;         610 AA.
P17312; Q9T0U4; Q9T0U5; Q9T0U6;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-AUG-1990, sequence version 1.
22-NOV-2017, entry version 108.
RecName: Full=Terminase, large subunit;
EC=3.1.-.- {ECO:0000269|PubMed:18627466, ECO:0000269|PubMed:8063105};
AltName: Full=DNA-packaging protein Gp17;
AltName: Full=Gene product 17;
Short=gp17;
Name=17;
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].
STRAIN=D;
PubMed=2374730; DOI=10.1093/nar/18.13.4005;
Powell D., Franklin J., Arisaka F., Mosig G.;
"Bacteriophage T4 DNA packaging genes 16 and 17.";
Nucleic Acids Res. 18:4005-4005(1990).
[2]
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).
[3]
FUNCTION.
PubMed=8063105; DOI=10.1016/0378-1119(94)90834-6;
Bhattacharyya S.P., Rao V.B.;
"Structural analysis of DNA cleaved in vivo by bacteriophage T4
terminase.";
Gene 146:67-72(1994).
[4]
CHARACTERIZATION.
PubMed=9533879; DOI=10.1006/jmbi.1998.1619;
Franklin J.L., Haseltine D., Davenport L., Mosig G.;
"The largest (70 kDa) product of the bacteriophage T4 DNA terminase
gene 17 binds to single-stranded DNA segments and digests them towards
junctions with double-stranded DNA.";
J. Mol. Biol. 277:541-557(1998).
[5]
INTERACTION WITH GP20.
PubMed=10366503; DOI=10.1006/jmbi.1999.2781;
Lin H., Rao V.B., Black L.W.;
"Analysis of capsid portal protein and terminase functional domains:
interaction sites required for DNA packaging in bacteriophage T4.";
J. Mol. Biol. 289:249-260(1999).
[6]
FUNCTION.
PubMed=12235385; DOI=10.1093/nar/gkf524;
Mitchell M.S., Matsuzaki S., Imai S., Rao V.B.;
"Sequence analysis of bacteriophage T4 DNA packaging/terminase genes
16 and 17 reveals a common ATPase center in the large subunit of viral
terminases.";
Nucleic Acids Res. 30:4009-4021(2002).
[7]
INTERACTION WITH GP55.
PubMed=12051907; DOI=10.1016/S0022-2836(02)00298-X;
Malys N., Chang D.Y., Baumann R.G., Xie D., Black L.W.;
"A bipartite bacteriophage T4 SOC and HOC randomized peptide display
library: detection and analysis of phage T4 terminase (gp17) and late
sigma factor (gp55) interaction.";
J. Mol. Biol. 319:289-304(2002).
[8]
INTERACTION WITH GP16.
PubMed=12466275; DOI=10.1074/jbc.M208574200;
Baumann R.G., Black L.W.;
"Isolation and characterization of T4 bacteriophage gp17 terminase, a
large subunit multimer with enhanced ATPase activity.";
J. Biol. Chem. 278:4618-4627(2003).
[9]
CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, AND MUTAGENESIS OF ASP-401;
GLU-404; GLY-405; ASP-409; GLU-458 AND ASP-542.
PubMed=18627466; DOI=10.1111/j.1365-2958.2008.06344.x;
Alam T.I., Draper B., Kondabagil K., Rentas F.J., Ghosh-Kumar M.,
Sun S., Rossmann M.G., Rao V.B.;
"The headful packaging nuclease of bacteriophage T4.";
Mol. Microbiol. 69:1180-1190(2008).
[10]
REVIEW.
PubMed=18687036; DOI=10.1146/annurev.genet.42.110807.091545;
Rao V.B., Feiss M.;
"The bacteriophage DNA packaging motor.";
Annu. Rev. Genet. 42:647-681(2008).
[11]
X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 1-360.
PubMed=17386269; DOI=10.1016/j.molcel.2007.02.013;
Sun S., Kondabagil K., Gentz P.M., Rossmann M.G., Rao V.B.;
"The structure of the ATPase that powers DNA packaging into
bacteriophage T4 procapsids.";
Mol. Cell 25:943-949(2007).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-567, AND COFACTOR.
PubMed=19109896; DOI=10.1016/j.cell.2008.11.015;
Sun S., Kondabagil K., Draper B., Alam T.I., Bowman V.D., Zhang Z.,
Hegde S., Fokine A., Rossmann M.G., Rao V.B.;
"The structure of the phage T4 DNA packaging motor suggests a
mechanism dependent on electrostatic forces.";
Cell 135:1251-1262(2008).
-!- FUNCTION: The terminase large subunit acts as an ATP driven
molecular motor necessary for viral DNA translocation into empty
capsids and as an endonuclease that cuts the viral genome to
initiate and to end a packaging reaction. The terminase lies at a
unique vertex of the procapsid and is composed of two subunits, a
small terminase subunit involved in viral DNA recognition
(packaging sequence), and a large terminase subunit possessing
endonucleolytic and ATPase activities. Both terminase subunits
heterooligomerize and are docked on the portal protein to form the
packaging machine. The terminase large subunit exhibits
endonuclease activity and cleaves the viral genome concatemer once
the capsid is full (headful packaging). Once the capsid is
packaged with the DNA, the terminase complex is substituted by
neck proteins. {ECO:0000269|PubMed:12235385,
ECO:0000269|PubMed:8063105}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:18627466,
ECO:0000305|PubMed:19109896};
Note=Binds 2 Mg(2+) ions per subunit.
{ECO:0000305|PubMed:18627466, ECO:0000305|PubMed:19109896};
-!- SUBUNIT: Interacts with the terminase small subunit gp16; the
active complex is probably heterooligomeric. Interacts with the
portal protein gp20. Interacts with gp55.
{ECO:0000269|PubMed:10366503, ECO:0000269|PubMed:12051907,
ECO:0000269|PubMed:12466275}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=4;
Name=Gp17;
IsoId=P17312-1; Sequence=Displayed;
Name=Gp17'A;
IsoId=P17312-2; Sequence=VSP_018679;
Name=Gp17'B;
IsoId=P17312-3; Sequence=VSP_018680;
Name=Gp17'';
IsoId=P17312-4; Sequence=VSP_018681;
-!- SIMILARITY: Belongs to the T4likevirus large terminase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X52394; CAA36641.1; -; Genomic_DNA.
EMBL; AF158101; AAD42422.1; -; Genomic_DNA.
EMBL; AF158101; AAD42684.1; -; Genomic_DNA.
EMBL; AF158101; AAD42685.1; -; Genomic_DNA.
EMBL; AF158101; AAD42686.1; -; Genomic_DNA.
PIR; JU0287; GVBPT4.
RefSeq; NP_049776.1; NC_000866.4. [P17312-1]
RefSeq; NP_049777.1; NC_000866.4. [P17312-2]
RefSeq; NP_049778.1; NC_000866.4. [P17312-3]
RefSeq; NP_049779.1; NC_000866.4. [P17312-4]
PDB; 2O0H; X-ray; 1.88 A; A=1-360.
PDB; 2O0J; X-ray; 1.80 A; A=1-360.
PDB; 2O0K; X-ray; 2.50 A; A=1-360.
PDB; 3CPE; X-ray; 2.80 A; A=1-567.
PDB; 3EZK; EM; 34.00 A; A/B/C/D/E=1-577.
PDBsum; 2O0H; -.
PDBsum; 2O0J; -.
PDBsum; 2O0K; -.
PDBsum; 3CPE; -.
PDBsum; 3EZK; -.
ProteinModelPortal; P17312; -.
SMR; P17312; -.
DIP; DIP-60322N; -.
IntAct; P17312; 1.
GeneID; 1258545; -.
GeneID; 1258647; -.
GeneID; 1258656; -.
GeneID; 1258675; -.
KEGG; vg:1258545; -.
KEGG; vg:1258647; -.
KEGG; vg:1258656; -.
KEGG; vg:1258675; -.
KO; K21523; -.
OrthoDB; VOG0900003S; -.
EvolutionaryTrace; P17312; -.
Proteomes; UP000009087; Genome.
GO; GO:0098009; C:viral terminase, large subunit; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004518; F:nuclease activity; IDA:UniProtKB.
GO; GO:0032359; P:provirus excision; IEA:UniProtKB-KW.
GO; GO:0019072; P:viral genome packaging; IDA:UniProtKB.
GO; GO:0046797; P:viral procapsid maturation; IDA:CACAO.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR035421; Terminase_6C.
Pfam; PF17289; Terminase_6C; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; ATP-binding; Complete proteome;
Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
Reference proteome; Viral genome excision; Viral genome packaging;
Viral release from host cell.
CHAIN 1 610 Terminase, large subunit.
/FTId=PRO_0000003331.
NP_BIND 299 306 ATP. {ECO:0000255}.
REGION 131 301 ATPase. {ECO:0000269|PubMed:12235385}.
REGION 322 331 Binding to the portal.
{ECO:0000269|PubMed:12235385}.
REGION 360 559 Nuclease. {ECO:0000269|PubMed:12235385}.
REGION 560 567 Binding to the portal.
{ECO:0000269|PubMed:12235385}.
MOTIF 160 167 Walker A motif.
MOTIF 251 256 Walker B motif.
ACT_SITE 256 256 For ATPase activity. {ECO:0000255}.
METAL 401 401 Magnesium 1; catalytic; for nuclease
activity. {ECO:0000305|PubMed:18627466}.
METAL 401 401 Magnesium 2; catalytic; for nuclease
activity. {ECO:0000305|PubMed:18627466}.
METAL 458 458 Magnesium 2; catalytic; for nuclease
activity. {ECO:0000305|PubMed:18627466}.
METAL 542 542 Magnesium 1; catalytic; for nuclease
activity. {ECO:0000305|PubMed:18627466}.
SITE 409 409 Modulates nuclease activity.
{ECO:0000269|PubMed:18627466}.
VAR_SEQ 1 194 Missing (in isoform Gp17'').
{ECO:0000305}.
/FTId=VSP_018681.
VAR_SEQ 1 105 Missing (in isoform Gp17'B).
{ECO:0000305}.
/FTId=VSP_018680.
VAR_SEQ 1 87 Missing (in isoform Gp17'A).
{ECO:0000305}.
/FTId=VSP_018679.
MUTAGEN 401 401 D->N: Complete loss of nuclease activity.
Almost no circular DNA packaging.
{ECO:0000269|PubMed:18627466}.
MUTAGEN 404 404 E->N: Complete loss of nuclease activity.
Almost no circular DNA packaging.
{ECO:0000269|PubMed:18627466}.
MUTAGEN 405 405 G->V: Complete loss of nuclease activity.
Almost no circular DNA packaging.
{ECO:0000269|PubMed:18627466}.
MUTAGEN 409 409 D->N: Enhanced nuclease activity. Normal
circular DNA packaging.
{ECO:0000269|PubMed:18627466}.
MUTAGEN 458 458 E->A: Complete loss of nuclease activity.
{ECO:0000269|PubMed:18627466}.
MUTAGEN 542 542 D->A: Complete loss of nuclease activity.
Unable to package circular plasmid DNA
but packages linear DNA.
{ECO:0000269|PubMed:18627466}.
HELIX 13 15 {ECO:0000244|PDB:2O0K}.
STRAND 17 19 {ECO:0000244|PDB:2O0K}.
HELIX 25 27 {ECO:0000244|PDB:2O0J}.
STRAND 30 33 {ECO:0000244|PDB:2O0J}.
STRAND 36 40 {ECO:0000244|PDB:2O0J}.
TURN 42 44 {ECO:0000244|PDB:2O0J}.
STRAND 47 51 {ECO:0000244|PDB:2O0J}.
HELIX 52 57 {ECO:0000244|PDB:2O0J}.
STRAND 67 69 {ECO:0000244|PDB:2O0J}.
HELIX 71 73 {ECO:0000244|PDB:2O0H}.
TURN 74 76 {ECO:0000244|PDB:2O0J}.
STRAND 85 87 {ECO:0000244|PDB:2O0J}.
STRAND 90 95 {ECO:0000244|PDB:2O0J}.
HELIX 104 115 {ECO:0000244|PDB:2O0J}.
HELIX 117 124 {ECO:0000244|PDB:2O0J}.
STRAND 126 128 {ECO:0000244|PDB:2O0J}.
STRAND 130 132 {ECO:0000244|PDB:2O0J}.
STRAND 134 136 {ECO:0000244|PDB:2O0J}.
HELIX 141 152 {ECO:0000244|PDB:2O0J}.
STRAND 153 160 {ECO:0000244|PDB:2O0J}.
STRAND 162 164 {ECO:0000244|PDB:2O0J}.
HELIX 166 179 {ECO:0000244|PDB:2O0J}.
STRAND 180 183 {ECO:0000244|PDB:2O0J}.
STRAND 185 192 {ECO:0000244|PDB:2O0J}.
HELIX 193 209 {ECO:0000244|PDB:2O0J}.
TURN 212 214 {ECO:0000244|PDB:2O0J}.
STRAND 218 221 {ECO:0000244|PDB:2O0J}.
STRAND 223 228 {ECO:0000244|PDB:2O0J}.
STRAND 233 238 {ECO:0000244|PDB:2O0J}.
HELIX 241 245 {ECO:0000244|PDB:2O0J}.
STRAND 250 256 {ECO:0000244|PDB:2O0J}.
HELIX 257 259 {ECO:0000244|PDB:2O0J}.
HELIX 263 275 {ECO:0000244|PDB:2O0J}.
TURN 276 278 {ECO:0000244|PDB:2O0K}.
STRAND 281 286 {ECO:0000244|PDB:2O0J}.
STRAND 290 292 {ECO:0000244|PDB:2O0J}.
HELIX 293 302 {ECO:0000244|PDB:2O0J}.
STRAND 305 307 {ECO:0000244|PDB:2O0K}.
STRAND 309 313 {ECO:0000244|PDB:2O0J}.
HELIX 315 317 {ECO:0000244|PDB:2O0J}.
HELIX 319 322 {ECO:0000244|PDB:2O0J}.
STRAND 327 329 {ECO:0000244|PDB:2O0J}.
HELIX 333 341 {ECO:0000244|PDB:2O0J}.
HELIX 345 352 {ECO:0000244|PDB:2O0J}.
STRAND 361 364 {ECO:0000244|PDB:3CPE}.
HELIX 366 369 {ECO:0000244|PDB:3CPE}.
STRAND 381 388 {ECO:0000244|PDB:3CPE}.
STRAND 396 401 {ECO:0000244|PDB:3CPE}.
STRAND 404 406 {ECO:0000244|PDB:3CPE}.
STRAND 411 417 {ECO:0000244|PDB:3CPE}.
STRAND 419 434 {ECO:0000244|PDB:3CPE}.
TURN 436 438 {ECO:0000244|PDB:3CPE}.
HELIX 439 449 {ECO:0000244|PDB:3CPE}.
STRAND 455 460 {ECO:0000244|PDB:3CPE}.
HELIX 461 471 {ECO:0000244|PDB:3CPE}.
STRAND 482 485 {ECO:0000244|PDB:3CPE}.
STRAND 487 490 {ECO:0000244|PDB:3CPE}.
HELIX 493 508 {ECO:0000244|PDB:3CPE}.
STRAND 511 513 {ECO:0000244|PDB:3CPE}.
HELIX 517 523 {ECO:0000244|PDB:3CPE}.
STRAND 525 529 {ECO:0000244|PDB:3CPE}.
STRAND 532 535 {ECO:0000244|PDB:3CPE}.
HELIX 542 555 {ECO:0000244|PDB:3CPE}.
HELIX 557 559 {ECO:0000244|PDB:3CPE}.
SEQUENCE 610 AA; 69756 MW; 5BC2F4BEC3EC79E4 CRC64;
MEQPINVLND FHPLNEAGKI LIKHPSLAER KDEDGIHWIK SQWDGKWYPE KFSDYLRLHK
IVKIPNNSDK PELFQTYKDK NNKRSRYMGL PNLKRANIKT QWTREMVEEW KKCRDDIVYF
AETYCAITHI DYGVIKVQLR DYQRDMLKIM SSKRMTVCNL SRQLGKTTVV AIFLAHFVCF
NKDKAVGILA HKGSMSAEVL DRTKQAIELL PDFLQPGIVE WNKGSIELDN GSSIGAYASS
PDAVRGNSFA MIYIDECAFI PNFHDSWLAI QPVISSGRRS KIIITTTPNG LNHFYDIWTA
AVEGKSGFEP YTAIWNSVKE RLYNDEDIFD DGWQWSIQTI NGSSLAQFRQ EHTAAFEGTS
GTLISGMKLA VMDFIEVTPD DHGFHQFKKP EPDRKYIATL DCSEGRGQDY HALHIIDVTD
DVWEQVGVLH SNTISHLILP DIVMRYLVEY NECPVYIELN STGVSVAKSL YMDLEYEGVI
CDSYTDLGMK QTKRTKAVGC STLKDLIEKD KLIIHHRATI QEFRTFSEKG VSWAAEEGYH
DDLVMSLVIF GWLSTQSKFI DYADKDDMRL ASEVFSKELQ DMSDDYAPVI FVDSVHSAEY
VPVSHGMSMV


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