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Protein

Sliding-clamp-loader gp44 subunit

Gene

62

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Function as a sliding-clamp-loading ATPase enzyme during DNA replication. Required for elongation of primed templates by controlling the polymerase processivity. Progressive binding of ATPs triggers a conformational change in the complex that inhibits ATPase activity.

GO - Molecular functioni

GO - Biological processi

  • bidirectional double-stranded viral DNA replication Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Sliding-clamp-loader gp44 subunit
Alternative name(s):
Clamp loader small subunit
Gene product 62
Short name:
gp62
Gene namesi
Name:62
OrganismiEnterobacteria phage T4 (Bacteriophage T4)
Taxonomic identifieri10665 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000009087 Componenti: Genome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 187187Sliding-clamp-loader gp44 subunitPRO_0000164929Add
BLAST

Interactioni

Subunit structurei

Heterodimer of gp44 and gp62 that forms a complex with gp45 in the presence of ATP.

Chemistry

BindingDBiP04527.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 198Combined sources
Helixi22 – 3211Combined sources
Helixi36 – 4914Combined sources
Beta strandi55 – 584Combined sources
Helixi62 – 709Combined sources
Turni73 – 753Combined sources
Helixi76 – 849Combined sources
Turni85 – 884Combined sources
Helixi93 – 1019Combined sources
Helixi119 – 13113Combined sources
Helixi137 – 14711Combined sources
Turni148 – 1514Combined sources
Helixi152 – 1576Combined sources
Helixi164 – 1707Combined sources
Helixi175 – 1828Combined sources
Turni183 – 1853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U5ZX-ray3.50A/K2-187[»]
3U60X-ray3.34A2-187[»]
3U61X-ray3.20A2-187[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

KOiK18945.

Family and domain databases

InterProiIPR031868. Phage_clamp_A.
[Graphical view]
PfamiPF16790. Phage_clamp_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04527-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLFKDDIQL NEHQVAWYSK DWTAVQSAAD SFKEKAENEF FEIIGAINNK
60 70 80 90 100
TKCSIAQKDY SKFMVENALS QFPECMPAVY AMNLIGSGLS DEAHFNYLMA
110 120 130 140 150
AVPRGKRYGK WAKLVEDSTE VLIIKLLAKR YQVNTNDAIN YKSILTKNGK
160 170 180
LPLVLKELKG LVTDDFLKEV TKNVKEQKQL KKLALEW
Length:187
Mass (Da):21,363
Last modified:August 13, 1987 - v1
Checksum:i686C9E3D28B42E07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711Q → E in CAA25342 (PubMed:2786875).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10160 Genomic DNA. Translation: AAC05395.1.
X00769 Genomic DNA. Translation: CAA25342.1.
AF158101 Genomic DNA. Translation: AAD42513.1.
PIRiA04303. IDBPT4.
RefSeqiNP_049664.1. NC_000866.4.

Genome annotation databases

GeneIDi1258559.
KEGGivg:1258559.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10160 Genomic DNA. Translation: AAC05395.1.
X00769 Genomic DNA. Translation: CAA25342.1.
AF158101 Genomic DNA. Translation: AAD42513.1.
PIRiA04303. IDBPT4.
RefSeqiNP_049664.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3U5ZX-ray3.50A/K2-187[»]
3U60X-ray3.34A2-187[»]
3U61X-ray3.20A2-187[»]
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP04527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258559.
KEGGivg:1258559.

Phylogenomic databases

KOiK18945.

Family and domain databases

InterProiIPR031868. Phage_clamp_A.
[Graphical view]
PfamiPF16790. Phage_clamp_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Organization and structure of four T4 genes coding for DNA replication proteins."
    Spicer E.K., Konigsberg W.H.
    (In) Mathews C.K., Kutter E.M., Mosig G., Berget P.B. (eds.); Bacteriophage T4, pp.291-301, American Society for Microbiology, Washington D.C. (1983)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The 44P subunit of the T4 DNA polymerase accessory protein complex catalyzes ATP hydrolysis."
    Rush J., Lin T.C., Quinones M., Spicer E.K., Douglas I., Williams K.R., Konigsberg W.H.
    J. Biol. Chem. 264:10943-10953(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "In vitro reconstitution of the bacteriophage T4 clamp loader complex (gp44/62)."
    Janzen D.M., Torgov M.Y., Reddy M.K.
    J. Biol. Chem. 274:35938-35943(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GP44, FUNCTION.
  5. "Structural analyses of gp45 sliding clamp interactions during assembly of the bacteriophage T4 DNA polymerase holoenzyme. II. The Gp44/62 clamp loader interacts with a single defined face of the sliding clamp ring."
    Latham G.J., Bacheller D.J., Pietroni P., von Hippel P.H.
    J. Biol. Chem. 272:31677-31684(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GP45, FUNCTION.
  6. "How a DNA polymerase clamp loader opens a sliding clamp."
    Kelch B.A., Makino D.L., O'Donnell M., Kuriyan J.
    Science 334:1675-1680(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 2-187.

Entry informationi

Entry nameiDPA62_BPT4
AccessioniPrimary (citable) accession number: P04527
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: November 11, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.