CLAMP_BPR69
ID CLAMP_BPR69 Reviewed; 228 AA.
AC O80164; Q76XX6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Sliding clamp {ECO:0000255|HAMAP-Rule:MF_04161};
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};
DE AltName: Full=Gene product 45;
DE Short=gp45;
GN Name=45;
OS Escherichia phage RB69 (Bacteriophage RB69).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Mosigvirus.
OX NCBI_TaxID=12353;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9555879; DOI=10.1128/jb.180.8.2005-2013.1998;
RA Yeh L.-S., Hsu T., Karam J.D.;
RT "Divergence of a DNA replication gene cluster in the T4-related
RT bacteriophage RB69.";
RL J. Bacteriol. 180:2005-2013(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Petrov V., Nolan J., Chin D., Letarov A., Krisch H.M., Karam J.D.;
RT "Enterobacteria phage RB69 complete genome.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF COMPLEX WITH POLYMERASE, AND
RP FUNCTION.
RX PubMed=10535734; DOI=10.1016/s0092-8674(00)81647-5;
RA Shamoo Y., Steitz T.A.;
RT "Building a replisome from interacting pieces: sliding clamp complexed to a
RT peptide from DNA polymerase and a polymerase editing complex.";
RL Cell 99:155-166(1999).
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. Interaction with the
CC sliding-clamp-loader opens the sliding clamp so that it can be loaded
CC around the DNA template. During transcription, encircles the DNA and
CC tethers host RNA polymerase (RNAP) to it. {ECO:0000255|HAMAP-
CC Rule:MF_04161}.
CC -!- SUBUNIT: Homotrimer. Interacts with the viral DNA polymerase; this
CC interaction constitutes the polymerase holoenzyme. Interacts with the
CC sliding-clamp-loader; this interaction allows the sliding-clamp-loader
CC to open the sliding clamp. Interacts with the viral DNA ligase. Part of
CC the 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 Interacts with the viral RNA polymerase (RNAP). Part of the
CC transcription activation complex containing host RNAP, the viral RNA
CC polymerase sigma-like factor, the late transcription coactivator, and
CC the sliding clamp. {ECO:0000255|HAMAP-Rule:MF_04161}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae sliding clamp family.
CC {ECO:0000255|HAMAP-Rule:MF_04161}.
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DR EMBL; AF039565; AAC39310.1; -; Genomic_DNA.
DR EMBL; AY303349; AAP75962.1; -; Genomic_DNA.
DR RefSeq; NP_861750.1; NC_004928.1.
DR PDB; 1B77; X-ray; 2.10 A; A/B/C=1-228.
DR PDB; 1B8H; X-ray; 3.00 A; A/B/C=1-228.
DR PDBsum; 1B77; -.
DR PDBsum; 1B8H; -.
DR SMR; O80164; -.
DR GeneID; 1494176; -.
DR KEGG; vg:1494176; -.
DR EvolutionaryTrace; O80164; -.
DR Proteomes; UP000000876; Genome.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR GO; GO:0019083; P:viral transcription; IEA:UniProtKB-KW.
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_0000149228"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 36..48
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1B77"
FT HELIX 57..64
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:1B77"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:1B77"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1B77"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:1B77"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:1B77"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:1B77"
SQ SEQUENCE 228 AA; 25111 MW; 158C771A684E4666 CRC64;
MKLSKDTIAI LKNFASINSG ILLSQGKFIM TRAVNGTTYA EANISDEIDF DVALYDLNSF
LSILSLVSDD AEISMHTDGN IKIADTRSTV YWPAADKSTI VFPNKPIQFP VASVITEIKA
EDLQQLLRVS RGLQIDTIAI TNKDGKIVIN GYNKVEDSGL TRPKYSLTLT DYDGSNNFNF
VINMANMKIQ PGNYKVMLWG AGDKVAAKFE SSQVSYVIAM EADSTHDF
