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 24-JAN-2024, entry version 111. 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 Straboviridae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-30605; -. DR SMR; P04525; -. DR GeneID; 1258821; -. DR KEGG; vg:1258821; -. DR OrthoDB; 7567at10239; -. DR EvolutionaryTrace; P04525; -. DR Proteomes; UP000009087; Segment. 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 Gene3D; 3.70.10.10; -; 1. DR HAMAP; MF_04161; Sliding_clamp_T4; 1. DR InterPro; IPR046938; DNA_clamp_sf. 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. DR SUPFAM; SSF55979; DNA clamp; 2. 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 //