LOADL_BPT4
ID LOADL_BPT4 Reviewed; 319 AA.
AC P04526;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Sliding-clamp-loader large subunit {ECO:0000255|HAMAP-Rule:MF_04162};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04162, ECO:0000269|PubMed:18676368};
DE AltName: Full=Clamp loader gp44 subunit {ECO:0000255|HAMAP-Rule:MF_04162};
DE AltName: Full=Gene product 44;
DE Short=gp44;
GN Name=44;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6096371; DOI=10.1016/s0021-9258(17)42566-x;
RA Spicer E.K., Nossal N.G., Williams K.R.;
RT "Bacteriophage T4 gene 44 DNA polymerase accessory protein. Sequences of
RT gene 44 and its protein product.";
RL J. Biol. Chem. 259:15425-15432(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6473098; DOI=10.1093/nar/12.15.5979;
RA Trojanowska M., Miller E.S., Karam J., Stormo G., Gold L.;
RT "The bacteriophage T4 regA gene: primary sequence of a translational
RT repressor.";
RL Nucleic Acids Res. 12:5979-5993(1984).
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 SUBUNIT.
RX PubMed=2663867; DOI=10.1016/s0021-9258(18)63914-6;
RA Jarvis T.C., Paul L.S., von Hippel P.H.;
RT "Structural and enzymatic studies of the T4 DNA replication system. I.
RT Physical characterization of the polymerase accessory protein complex.";
RL J. Biol. Chem. 264:12709-12716(1989).
RN [5]
RP INTERACTION WITH THE SLIDING CLAMP.
RX PubMed=9395509; DOI=10.1074/jbc.272.50.31677;
RA Latham G.J., Bacheller D.J., Pietroni P., von Hippel P.H.;
RT "Structural analyses of gp45 sliding clamp interactions during assembly of
RT the bacteriophage T4 DNA polymerase holoenzyme. II. The Gp44/62 clamp
RT loader interacts with a single defined face of the sliding clamp ring.";
RL J. Biol. Chem. 272:31677-31684(1997).
RN [6]
RP SUBUNIT, AND FUNCTION.
RX PubMed=10585481; DOI=10.1074/jbc.274.50.35938;
RA Janzen D.M., Torgov M.Y., Reddy M.K.;
RT "In vitro reconstitution of the bacteriophage T4 clamp loader complex
RT (gp44/62).";
RL J. Biol. Chem. 274:35938-35943(1999).
RN [7]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=16800623; DOI=10.1021/bi0601205;
RA Zhuang Z., Berdis A.J., Benkovic S.J.;
RT "An alternative clamp loading pathway via the T4 clamp loader gp44/62-DNA
RT complex.";
RL Biochemistry 45:7976-7989(2006).
RN [8]
RP IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=16800624; DOI=10.1021/bi0603322;
RA Smiley R.D., Zhuang Z., Benkovic S.J., Hammes G.G.;
RT "Single-molecule investigation of the T4 bacteriophage DNA polymerase
RT holoenzyme: multiple pathways of holoenzyme formation.";
RL Biochemistry 45:7990-7997(2006).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18676368; DOI=10.1074/jbc.m804371200;
RA Pietroni P., von Hippel P.H.;
RT "Multiple ATP binding is required to stabilize the 'activated' (clamp open)
RT clamp loader of the T4 DNA replication complex.";
RL J. Biol. Chem. 283:28338-28353(2008).
RN [10] {ECO:0007744|PDB:3U5Z, ECO:0007744|PDB:3U60, ECO:0007744|PDB:3U61}
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS), FUNCTION, AND INTERACTION WITH THE
RP SLIDING CLAMP.
RX PubMed=22194570; DOI=10.1126/science.1211884;
RA Kelch B.A., Makino D.L., O'Donnell M., Kuriyan J.;
RT "How a DNA polymerase clamp loader opens a sliding clamp.";
RL Science 334:1675-1680(2011).
CC -!- FUNCTION: Forms the sliding-clamp-loader together with the small
CC subunit (PubMed:10585481). Functions as an ATPase enzyme
CC (PubMed:16800623, PubMed:18676368). The clamp loader holds the clamp in
CC an open conformation and places it onto the DNA (PubMed:22194570,
CC PubMed:18676368). 4 ATP molecules must bind to the sliding-clamp-loader
CC before the latter can open the sliding clamp (PubMed:18676368). ATP
CC hydrolysis triggers the detachment of the sliding clamp from the
CC sliding-clamp-loader, freeing the sliding clamp to track along DNA
CC (PubMed:18676368, PubMed:22194570). {ECO:0000255|HAMAP-Rule:MF_04162,
CC ECO:0000269|PubMed:10585481, ECO:0000269|PubMed:16800623,
CC ECO:0000269|PubMed:18676368, ECO:0000269|PubMed:22194570}.
CC -!- SUBUNIT: The sliding-clamp-loader consists of 4 large subunits and 1
CC small subunit (PubMed:2663867, PubMed:10585481). Interacts with the
CC sliding clamp; this interaction allows the sliding-clamp-loader to open
CC the sliding clamp (PubMed:22194570, PubMed:9395509). Part of the
CC replicase complex that includes the DNA polymerase, the polymerase
CC clamp, the clamp loader complex, the single-stranded DNA binding
CC protein, the primase, the helicase and the helicase assembly factor
CC (PubMed:16800624). {ECO:0000255|HAMAP-Rule:MF_04162,
CC ECO:0000269|PubMed:10585481, ECO:0000269|PubMed:16800624,
CC ECO:0000269|PubMed:22194570, ECO:0000269|PubMed:2663867,
CC ECO:0000269|PubMed:9395509}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae sliding-clamp-loader large
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_04162}.
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DR EMBL; X00769; CAA25341.1; -; Genomic_DNA.
DR EMBL; M10160; AAC05394.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42469.1; -; Genomic_DNA.
DR PIR; A04302; IDBPA4.
DR RefSeq; NP_049665.1; NC_000866.4.
DR PDB; 3U5Z; X-ray; 3.50 A; B/C/D/E/L/M/N/O=1-319.
DR PDB; 3U60; X-ray; 3.34 A; B/C/D/E=1-319.
DR PDB; 3U61; X-ray; 3.20 A; B/C/D/E=1-319.
DR PDBsum; 3U5Z; -.
DR PDBsum; 3U60; -.
DR PDBsum; 3U61; -.
DR SMR; P04526; -.
DR BindingDB; P04526; -.
DR GeneID; 1258787; -.
DR KEGG; vg:1258787; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003689; F:DNA clamp loader activity; IDA:UniProtKB.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04162; T4_Clamp_Loader_L; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR046388; T4_Clamp_Loader_L.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Hydrolase;
KW Nucleotide-binding; Reference proteome; Viral DNA replication.
FT CHAIN 1..319
FT /note="Sliding-clamp-loader large subunit"
FT /id="PRO_0000164927"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162,
FT ECO:0000269|PubMed:22194570"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162,
FT ECO:0000269|PubMed:22194570"
FT BINDING 53..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162,
FT ECO:0000269|PubMed:22194570"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162,
FT ECO:0000269|PubMed:22194570"
FT CONFLICT 132
FT /note="C -> S (in Ref. 2; CAA25341)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="R -> G (in Ref. 2; CAA25341)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="S -> T (in Ref. 2; CAA25341)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="R -> A (in Ref. 2; CAA25341)"
FT /evidence="ECO:0000305"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 27..38
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3U60"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 81..85
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 87..93
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 115..128
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 162..183
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3U60"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3U60"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 247..257
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:3U5Z"
FT HELIX 261..275
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 278..294
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 301..315
FT /evidence="ECO:0007829|PDB:3U61"
SQ SEQUENCE 319 AA; 35786 MW; B912551C4FF49578 CRC64;
MITVNEKEHI LEQKYRPSTI DECILPAFDK ETFKSITSKG KIPHIILHSP SPGTGKTTVA
KALCHDVNAD MMFVNGSDCK IDFVRGPLTN FASAASFDGR QKVIVIDEFD RSGLAESQRH
LRSFMEAYSS NCSIIITANN IDGIIKPLQS RCRVITFGQP TDEDKIEMMK QMIRRLTEIC
KHEGIAIADM KVVAALVKKN FPDFRKTIGE LDSYSSKGVL DAGILSLVTN DRGAIDDVLE
SLKNKDVKQL RALAPKYAAD YSWFVGKLAE EIYSRVTPQS IIRMYEIVGE NNQYHGIAAN
TELHLAYLFI QLACEMQWK
