LOADS_BPT4
ID LOADS_BPT4 Reviewed; 187 AA.
AC P04527;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Sliding-clamp-loader small subunit {ECO:0000255|HAMAP-Rule:MF_04163};
DE AltName: Full=Clamp loader gp62 subunit {ECO:0000255|HAMAP-Rule:MF_04163};
DE AltName: Full=Gene product 62;
DE Short=gp62;
GN Name=62;
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].
RA Spicer E.K., Konigsberg W.H.;
RT "Organization and structure of four T4 genes coding for DNA replication
RT proteins.";
RL (In) Mathews C.K., Kutter E.M., Mosig G., Berget P.B. (eds.);
RL Bacteriophage T4, pp.291-301, American Society for Microbiology, Washington
RL D.C. (1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2786875; DOI=10.1016/s0021-9258(18)60410-7;
RA Rush J., Lin T.C., Quinones M., Spicer E.K., Douglas I., Williams K.R.,
RA Konigsberg W.H.;
RT "The 44P subunit of the T4 DNA polymerase accessory protein complex
RT catalyzes ATP hydrolysis.";
RL J. Biol. Chem. 264:10943-10953(1989).
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 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 [6]
RP INTERACTION WITH THE SLIDING CLAMP, AND FUNCTION.
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 [7]
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 [8] {ECO:0007744|PDB:3U5Z, ECO:0007744|PDB:3U60, ECO:0007744|PDB:3U61}
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 2-187, AND FUNCTION.
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). The clamp loader holds the clamp in an open
CC conformation and places it onto the DNA (PubMed:22194570).
CC {ECO:0000255|HAMAP-Rule:MF_04163, ECO:0000269|PubMed:10585481,
CC 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). 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 {ECO:0000255|HAMAP-Rule:MF_04163, ECO:0000269|PubMed:10585481,
CC ECO:0000269|PubMed:16800624, ECO:0000269|PubMed:22194570,
CC ECO:0000269|PubMed:2663867}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae sliding-clamp-loader small
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_04163}.
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DR EMBL; M10160; AAC05395.1; -; Genomic_DNA.
DR EMBL; X00769; CAA25342.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42513.1; -; Genomic_DNA.
DR PIR; A04303; IDBPT4.
DR RefSeq; NP_049664.1; NC_000866.4.
DR PDB; 3U5Z; X-ray; 3.50 A; A/K=2-187.
DR PDB; 3U60; X-ray; 3.34 A; A=2-187.
DR PDB; 3U61; X-ray; 3.20 A; A=2-187.
DR PDBsum; 3U5Z; -.
DR PDBsum; 3U60; -.
DR PDBsum; 3U61; -.
DR SMR; P04527; -.
DR BindingDB; P04527; -.
DR GeneID; 1258559; -.
DR KEGG; vg:1258559; -.
DR Proteomes; UP000009087; Genome.
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 HAMAP; MF_04163; T4_Clamp_Loader_S; 1.
DR InterPro; IPR031868; Phage_clamp_gp62.
DR Pfam; PF16790; Phage_clamp_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; Reference proteome;
KW Viral DNA replication.
FT CHAIN 1..187
FT /note="Sliding-clamp-loader small subunit"
FT /id="PRO_0000164929"
FT CONFLICT 71
FT /note="Q -> E (in Ref. 2; CAA25342)"
FT /evidence="ECO:0000305"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:3U61"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3U5Z"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:3U61"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:3U61"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3U61"
SQ SEQUENCE 187 AA; 21363 MW; 686C9E3D28B42E07 CRC64;
MSLFKDDIQL NEHQVAWYSK DWTAVQSAAD SFKEKAENEF FEIIGAINNK TKCSIAQKDY
SKFMVENALS QFPECMPAVY AMNLIGSGLS DEAHFNYLMA AVPRGKRYGK WAKLVEDSTE
VLIIKLLAKR YQVNTNDAIN YKSILTKNGK LPLVLKELKG LVTDDFLKEV TKNVKEQKQL
KKLALEW
