CLAMP_BPT4
ID CLAMP_BPT4 Reviewed; 228 AA.
AC P04525; Q9T0Q0;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Sliding clamp {ECO:0000255|HAMAP-Rule:MF_04161, ECO:0000303|PubMed:26735934};
DE AltName: Full=DNA polymerase accessory protein Gp45 {ECO:0000255|HAMAP-Rule:MF_04161};
DE AltName: Full=DNA polymerase clamp {ECO:0000255|HAMAP-Rule:MF_04161, ECO:0000303|PubMed:16800624};
DE AltName: Full=Gene product 45;
DE Short=gp45;
DE AltName: Full=Sliding clamp Gp45 {ECO:0000303|PubMed:33602900};
GN Name=45;
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=6284751; DOI=10.1016/s0021-9258(18)34228-5;
RA Spicer E.K., Noble J.A., Nossal N.G., Konigsberg W.H., Williams K.R.;
RT "Bacteriophage T4 gene 45. Sequences of the structural gene and its protein
RT product.";
RL J. Biol. Chem. 257:8972-8979(1982).
RN [2]
RP SEQUENCE REVISION TO 69; 100 AND 129.
RA Spicer E.K.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=3543399; DOI=10.1128/jvi.61.2.366-374.1987;
RA Hsu T., Wei R., Dawson M., Karam J.D.;
RT "Identification of two new bacteriophage T4 genes that may have roles in
RT transcription and DNA replication.";
RL J. Virol. 61:366-374(1987).
RN [5]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=8475061; DOI=10.1073/pnas.90.8.3211;
RA Reddy M.K., Weitzel S.E., von Hippel P.H.;
RT "Assembly of a functional replication complex without ATP hydrolysis: a
RT direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3211-3215(1993).
RN [6]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=9395510; DOI=10.1074/jbc.272.50.31685;
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. III. The Gp43 DNA
RT polymerase binds to the same face of the sliding clamp as the clamp
RT loader.";
RL J. Biol. Chem. 272:31685-31692(1997).
RN [7]
RP FUNCTION.
RX PubMed=10535942; DOI=10.1073/pnas.96.22.12448;
RA Latham G.J., Dong F., Pietroni P., Dozono J.M., Bacheller D.J.,
RA von Hippel P.H.;
RT "Opening of a monomer-monomer interface of the trimeric bacteriophage T4-
RT coded GP45 sliding clamp is required for clamp loading onto DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12448-12453(1999).
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 REVIEW, AND IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=26102578; DOI=10.3390/v7062766;
RA Noble E., Spiering M.M., Benkovic S.J.;
RT "Coordinated DNA replication by the bacteriophage T4 replisome.";
RL Viruses 7:3186-3200(2015).
RN [10]
RP SUBUNIT.
RX PubMed=26735934; DOI=10.1021/acs.biochem.5b01204;
RA Singh M.I., Jain V.;
RT "Molecular dissection of the homotrimeric sliding clamp of T4 Phage: two
RT domains of a subunit display asymmetric characteristics.";
RL Biochemistry 55:588-596(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
RX PubMed=10698628; DOI=10.1006/jmbi.1999.3511;
RA Moarefi I., Jeruzalmi D., Turner J., O'Donnell M., Kuriyan J.;
RT "Crystal structure of the DNA polymerase processivity factor of T4
RT bacteriophage.";
RL J. Mol. Biol. 296:1215-1223(2000).
RN [12] {ECO:0007744|PDB:3U5Z, ECO:0007744|PDB:3U60, ECO:0007744|PDB:3U61}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS), FUNCTION, AND INTERACTION WITH THE
RP SLIDING-CLAMP-LOADER.
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).
RN [13] {ECO:0007744|PDB:6DRT}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS), INTERACTION WITH THE VIRAL DNA
RP LIGASE, AND SUBUNIT.
RX PubMed=30169742; DOI=10.1093/nar/gky776;
RA Shi K., Bohl T.E., Park J., Zasada A., Malik S., Banerjee S., Tran V.,
RA Li N., Yin Z., Kurniawan F., Orellana K., Aihara H.;
RT "T4 DNA ligase structure reveals a prototypical ATP-dependent ligase with a
RT unique mode of sliding clamp interaction.";
RL Nucleic Acids Res. 46:10474-10488(2018).
RN [14] {ECO:0007744|PDB:7D7D}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), IDENTIFICATION IN THE
RP TRANSCRIPTION ACTIVATION COMPLEX, INTERACTION WITH HOST RNA POLYMERASE, AND
RP FUNCTION.
RX PubMed=33602900; DOI=10.1038/s41467-021-21392-0;
RA Shi J., Wen A., Jin S., Gao B., Huang Y., Feng Y.;
RT "Transcription activation by a sliding clamp.";
RL Nat. Commun. 12:1131-1131(2021).
CC -!- FUNCTION: Sliding clamp that encircles the genomic DNA and links the
CC DNA polymerase to the template to control the processivity of DNA
CC synthesis. Responsible for tethering the catalytic subunit of DNA
CC polymerase to DNA during high-speed replication (PubMed:10535942).
CC Interaction with the sliding-clamp-loader opens the sliding clamp so
CC that it can be loaded around the DNA template (PubMed:22194570). During
CC transcription, encircles the DNA and tethers host RNA polymerase (RNAP)
CC to it (PubMed:33602900). {ECO:0000255|HAMAP-Rule:MF_04161,
CC ECO:0000269|PubMed:10535942, ECO:0000269|PubMed:22194570,
CC ECO:0000269|PubMed:33602900}.
CC -!- SUBUNIT: Homotrimer (PubMed:26735934, PubMed:30169742). Interacts with
CC the viral DNA polymerase; this interaction constitutes the polymerase
CC holoenzyme (PubMed:8475061, PubMed:9395510). Interacts with the
CC sliding-clamp-loader; this interaction allows the sliding-clamp-loader
CC to open the sliding clamp (PubMed:22194570). Interacts with the viral
CC DNA ligase (PubMed:30169742). Part of the replicase complex that
CC includes the DNA polymerase, the polymerase clamp, the clamp loader
CC complex, the single-stranded DNA binding protein, the primase, the
CC helicase and the helicase assembly factor (PubMed:16800624,
CC PubMed:26102578). Interacts with the viral RNA polymerase (RNAP)
CC (PubMed:33602900). Part of the transcription activation complex
CC containing host RNAP, the viral RNA polymerase sigma-like factor, the
CC late transcription coactivator, and the sliding clamp
CC (PubMed:33602900). {ECO:0000255|HAMAP-Rule:MF_04161,
CC ECO:0000269|PubMed:16800624, ECO:0000269|PubMed:22194570,
CC ECO:0000269|PubMed:26102578, ECO:0000269|PubMed:26735934,
CC ECO:0000269|PubMed:30169742, ECO:0000269|PubMed:33602900,
CC ECO:0000269|PubMed:8475061, ECO:0000269|PubMed:9395510}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae sliding clamp family.
CC {ECO:0000255|HAMAP-Rule:MF_04161}.
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DR EMBL; V01535; CAA24777.1; -; Genomic_DNA.
DR EMBL; M10160; AAC05393.1; -; Genomic_DNA.
DR EMBL; X00769; CAA25340.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42470.1; -; Genomic_DNA.
DR EMBL; M15080; AAA32519.1; -; Genomic_DNA.
DR PIR; A04301; IDBP44.
DR RefSeq; NP_049666.1; NC_000866.4.
DR PDB; 1CZD; X-ray; 2.45 A; A/B/C=1-228.
DR PDB; 3U5Z; X-ray; 3.50 A; F/G/H/P/Q/R=1-228.
DR PDB; 3U60; X-ray; 3.34 A; F/G/H=1-228.
DR PDB; 3U61; X-ray; 3.20 A; F/G/H=1-228.
DR PDB; 6DRT; X-ray; 2.12 A; A/B/C=1-228.
DR PDB; 7D7D; EM; 4.50 A; G/H/I=1-228.
DR PDBsum; 1CZD; -.
DR PDBsum; 3U5Z; -.
DR PDBsum; 3U60; -.
DR PDBsum; 3U61; -.
DR PDBsum; 6DRT; -.
DR PDBsum; 7D7D; -.
DR SMR; P04525; -.
DR GeneID; 1258821; -.
DR KEGG; vg:1258821; -.
DR EvolutionaryTrace; P04525; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IMP: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 GO; GO:0039693; P:viral DNA genome replication; IMP:UniProtKB.
DR GO; GO:0019083; P:viral transcription; IDA:UniProtKB.
DR HAMAP; MF_04161; Sliding_clamp_T4; 1.
DR InterPro; IPR004190; DNA_pol_proc_fac.
DR InterPro; IPR015200; Sliding_clamp_C.
DR InterPro; IPR046389; Sliding_clamp_T4.
DR Pfam; PF02916; DNA_PPF; 1.
DR Pfam; PF09116; gp45-slide_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; Reference proteome; Viral DNA replication;
KW Viral transcription.
FT CHAIN 1..228
FT /note="Sliding clamp"
FT /id="PRO_0000149229"
FT CONFLICT 69
FT /note="Missing (in Ref. 1; CAA24777)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> R (in Ref. 1; CAA24777/CAA25340/AAC05393)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="V -> D (in Ref. 1; CAA24777)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="V -> L (in Ref. 1; CAA24777)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 36..48
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:6DRT"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:6DRT"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6DRT"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:6DRT"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6DRT"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:6DRT"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6DRT"
SQ SEQUENCE 228 AA; 24858 MW; 765DF4AAB76D005B CRC64;
MKLSKDTTAL LKNFATINSG IMLKSGQFIM TRAVNGTTYA EANISDVIDF DVAIYDLNGF
LGILSLVNDD AEISQSEDGN IKIADARSTI FWPAADPSTV VAPNKPIPFP VASAVTEIKA
EDLQQLLRVS RGLQIDTIAI TVKEGKIVIN GFNKVEDSAL TRVKYSLTLG DYDGENTFNF
IINMANMKMQ PGNYKLLLWA KGKQGAAKFE GEHANYVVAL EADSTHDF
