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Protein

Single-stranded DNA-binding protein

Gene

32

Organism
Enterobacteria phage T4 (Bacteriophage T4)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds preferentially to single-stranded DNA and therefore, destabilizes double-stranded DNA. It is involved in DNA replication, repair and recombination. Binds ss-DNA as the replication fork advances and stimulates the replisome processivity and accuracy.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi64Zinc1
Metal bindingi77Zinc1
Metal bindingi87Zinc1
Metal bindingi90Zinc1

GO - Molecular functioni

GO - Biological processi

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

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Single-stranded DNA-binding protein
Alternative name(s):
Gp32
Helix-destabilizing protein
Gene namesi
Name:32
Synonyms:ssb
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)DescriptionActionsGraphical viewLength
ChainiPRO_00001650471 – 301Single-stranded DNA-binding proteinAdd BLAST301

Interactioni

Subunit structurei

Homodimer in the absence of DNA, monomer when binding DNA.

Structurei

Secondary structure

1301
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi26 – 28Combined sources3
Beta strandi41 – 47Combined sources7
Beta strandi51 – 55Combined sources5
Beta strandi57 – 68Combined sources12
Beta strandi71 – 76Combined sources6
Helixi78 – 81Combined sources4
Helixi88 – 95Combined sources8
Helixi98 – 101Combined sources4
Helixi103 – 109Combined sources7
Beta strandi112 – 123Combined sources12
Helixi128 – 130Combined sources3
Beta strandi134 – 139Combined sources6
Helixi141 – 148Combined sources8
Turni149 – 151Combined sources3
Helixi155 – 157Combined sources3
Turni167 – 169Combined sources3
Beta strandi173 – 180Combined sources8
Beta strandi183 – 185Combined sources3
Turni198 – 201Combined sources4
Helixi203 – 212Combined sources10
Helixi216 – 220Combined sources5
Helixi228 – 238Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPCX-ray2.20A22-239[»]
1WAImodel-S22-239[»]
ProteinModelPortaliP03695.
SMRiP03695.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03695.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni3 – 8LAST6

Domaini

The (Lys/Arg)3(Ser/Thr)2 (LAST) motif is involved in the cooperative binding of the protein to single-stranded nucleic acids.1 Publication

Keywords - Domaini

Zinc-finger

Phylogenomic databases

KOiK18946.

Family and domain databases

Gene3Di3.90.198.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR012339. Phage_T4_Gp32_ssDNA-bd.
[Graphical view]
PfamiPF08804. gp32. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequencei

Sequence statusi: Complete.

P03695-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRKSTAEL AAQMAKLNGN KGFSSEDKGE WKLKLDNAGN GQAVIRFLPS
60 70 80 90 100
KNDEQAPFAI LVNHGFKKNG KWYIETCSST HGDYDSCPVC QYISKNDLYN
110 120 130 140 150
TDNKEYSLVK RKTSYWANIL VVKDPAAPEN EGKVFKYRFG KKIWDKINAM
160 170 180 190 200
IAVDVEMGET PVDVTCPWEG ANFVLKVKQV SGFSNYDESK FLNQSAIPNI
210 220 230 240 250
DDESFQKELF EQMVDLSEMT SKDKFKSFEE LNTKFGQVMG TAVMGGAAAT
260 270 280 290 300
AAKKADKVAD DLDAFNVDDF NTKTEDDFMS SSSGSSSSAD DTDLDDLLND

L
Length:301
Mass (Da):33,506
Last modified:July 21, 1986 - v1
Checksum:i4C9771CF5D978487
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti86S → A AA sequence (PubMed:6257686).Curated1
Sequence conflicti91Q → E AA sequence (PubMed:6257686).Curated1
Sequence conflicti124D → N AA sequence (PubMed:6257686).Curated1
Sequence conflicti156E → Q AA sequence (PubMed:6257686).Curated1
Sequence conflicti194Q → E AA sequence (PubMed:6257686).Curated1
Sequence conflicti202D → N AA sequence (PubMed:6257686).Curated1
Sequence conflicti212Q → E AA sequence (PubMed:6257686).Curated1
Sequence conflicti223D → N AA sequence (PubMed:6257686).Curated1
Sequence conflicti276 – 277DD → NN AA sequence (PubMed:6257686).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti116 – 301Missing in mutant 32AMA453. Add BLAST186
Natural varianti292 – 296Missing in mutant delta PR201. 5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02513 Genomic DNA. Translation: AAA32511.1.
AF158101 Genomic DNA. Translation: AAD42454.1.
S54962 Genomic DNA. Translation: AAB25300.1.
PIRiA93924. DDBP34.
RefSeqiNP_049854.1. NC_000866.4.

Genome annotation databases

GeneIDi1258602.
KEGGivg:1258602.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J02513 Genomic DNA. Translation: AAA32511.1.
AF158101 Genomic DNA. Translation: AAD42454.1.
S54962 Genomic DNA. Translation: AAB25300.1.
PIRiA93924. DDBP34.
RefSeqiNP_049854.1. NC_000866.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GPCX-ray2.20A22-239[»]
1WAImodel-S22-239[»]
ProteinModelPortaliP03695.
SMRiP03695.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1258602.
KEGGivg:1258602.

Phylogenomic databases

KOiK18946.

Miscellaneous databases

EvolutionaryTraceiP03695.

Family and domain databases

Gene3Di3.90.198.10. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR012339. Phage_T4_Gp32_ssDNA-bd.
[Graphical view]
PfamiPF08804. gp32. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiVHED_BPT4
AccessioniPrimary (citable) accession number: P03695
Secondary accession number(s): Q38555
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

Interacts with the polymerase and the uvsX and uvsY proteins. Binds tightly to dDA protein.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.