LOADL_BPR69
ID LOADL_BPR69 Reviewed; 320 AA.
AC O64301; Q76XX7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
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 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.
CC -!- FUNCTION: Forms the sliding-clamp-loader together with the small
CC subunit. Functions as an ATPase enzyme. The clamp loader holds the
CC clamp in an open conformation and places it onto the DNA. 4 ATP
CC molecules must bind to the sliding-clamp-loader before the latter can
CC open the sliding clamp. ATP hydrolysis triggers the detachment of the
CC sliding clamp from the sliding-clamp-loader, freeing the sliding clamp
CC to track along DNA. {ECO:0000255|HAMAP-Rule:MF_04162}.
CC -!- SUBUNIT: The sliding-clamp-loader consists of 4 large subunits and 1
CC small subunit. Interacts with the sliding clamp; this interaction
CC allows the sliding-clamp-loader to open the sliding clamp. 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 {ECO:0000255|HAMAP-Rule:MF_04162}.
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; AF039565; AAC39311.1; -; Genomic_DNA.
DR EMBL; AY303349; AAP75961.1; -; Genomic_DNA.
DR RefSeq; NP_861749.1; NC_004928.1.
DR SMR; O64301; -.
DR PRIDE; O64301; -.
DR GeneID; 1494175; -.
DR KEGG; vg:1494175; -.
DR Proteomes; UP000000876; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome 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 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome; Viral DNA replication.
FT CHAIN 1..320
FT /note="Sliding-clamp-loader large subunit"
FT /id="PRO_0000164928"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162"
FT BINDING 53..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04162"
SQ SEQUENCE 320 AA; 36043 MW; 3EB83BE9C4BDB609 CRC64;
MITINSKEHI LEQKYRPSSI DECILPAYDH ETFKSLVSKG KLPHIILHSP SPGTGKTTVA
KALCNDINAE MMFVNGSDCK IDFVRGPLTA FARSVSMEGK PKVIVIDEFD RSGLAESQRH
LRTFMEEFSS NCSIIITANN IDGIIEPLRS RCRVIEFGRP TEEDKISMMK KMIHRMVEIC
KNENIEIADM KVVAALVKKN FPDFRRTIGQ LDQYSSKGVL DAGILSIVTN DRGTVSDVIE
AMKNKDIKQL RALAPKYAAD YSWFIDKLVS ECYDQVAPGK SIISLYEIAG ENNKFHGLAS
NIELHVMYML LQLTCELTWK
