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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Zinc
Metal bindingi77 – 771Zinc
Metal bindingi87 – 871Zinc
Metal bindingi90 – 901Zinc

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 301301Single-stranded DNA-binding proteinPRO_0000165047Add
BLAST

Interactioni

Subunit structurei

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

Structurei

Secondary structure

1
301
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi26 – 283Combined sources
Beta strandi41 – 477Combined sources
Beta strandi51 – 555Combined sources
Beta strandi57 – 6812Combined sources
Beta strandi71 – 766Combined sources
Helixi78 – 814Combined sources
Helixi88 – 958Combined sources
Helixi98 – 1014Combined sources
Helixi103 – 1097Combined sources
Beta strandi112 – 12312Combined sources
Helixi128 – 1303Combined sources
Beta strandi134 – 1396Combined sources
Helixi141 – 1488Combined sources
Turni149 – 1513Combined sources
Helixi155 – 1573Combined sources
Turni167 – 1693Combined sources
Beta strandi173 – 1808Combined sources
Beta strandi183 – 1853Combined sources
Turni198 – 2014Combined sources
Helixi203 – 21210Combined sources
Helixi216 – 2205Combined sources
Helixi228 – 23811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPCX-ray2.20A22-239[»]
1WAImodel-S22-239[»]
ProteinModelPortaliP03695.
SMRiP03695. Positions 22-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03695.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 86LAST

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861S → A AA sequence (PubMed:6257686).Curated
Sequence conflicti91 – 911Q → E AA sequence (PubMed:6257686).Curated
Sequence conflicti124 – 1241D → N AA sequence (PubMed:6257686).Curated
Sequence conflicti156 – 1561E → Q AA sequence (PubMed:6257686).Curated
Sequence conflicti194 – 1941Q → E AA sequence (PubMed:6257686).Curated
Sequence conflicti202 – 2021D → N AA sequence (PubMed:6257686).Curated
Sequence conflicti212 – 2121Q → E AA sequence (PubMed:6257686).Curated
Sequence conflicti223 – 2231D → N AA sequence (PubMed:6257686).Curated
Sequence conflicti276 – 2772DD → NN AA sequence (PubMed:6257686).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 301186Missing in mutant 32AMA453.
Add
BLAST
Natural varianti292 – 2965Missing in mutant delta PR201.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
1GPCX-ray2.20A22-239[»]
1WAImodel-S22-239[»]
ProteinModelPortaliP03695.
SMRiP03695. Positions 22-239.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequences involved in bacteriophage T4 gene 32 translational self-regulation."
    Krisch H.M., Allet B.
    Proc. Natl. Acad. Sci. U.S.A. 79:4937-4941(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AMBER MUTANT 32AMA453).
  2. "Primary structure of the bacteriophage T4 DNA helix-destabilizing protein."
    Williams K.R., Lopresti M.B., Setoguchi M.
    J. Biol. Chem. 256:1754-1762(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Amino acid sequence studies on T4 gene 32 DNA-binding proteins."
    Pan Y.-C.E., Nakashima Y., Sharief F.S., Li S.S.-L.
    Hoppe-Seyler's Z. Physiol. Chem. 361:1139-1153(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 1-74 AND 94-282.
  5. "Assembly of the bacteriophage T4 replication machine requires the acidic carboxy terminus of gene 32 protein."
    Hurley J.M., Chervitz S.A., Jarvis T.C., Singer B.S., Gold L.
    J. Mol. Biol. 229:398-418(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 213-301 (MUTANT DELTA PR201).
  6. "Zn(II) coordination domain mutants of T4 gene 32 protein."
    Giedroc D.P., Qiu H., Khan R., King G.C., Chen K.
    Biochemistry 31:765-774(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC-LIGANDS.
  7. "Structural basis for the nucleic acid binding cooperativity of bacteriophage T4 gene 32 protein: the (Lys/Arg)3(Ser/Thr)2 (LAST) motif."
    Casas-Finet J.R., Fischer K.R., Karpel R.L.
    Proc. Natl. Acad. Sci. U.S.A. 89:1050-1054(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN LAST.
  8. "Crystal structure of a replication fork single-stranded DNA binding protein (T4 gp32) complexed to DNA."
    Shamoo Y., Friedman A.M., Parsons M.R., Konigsberg W.H., Steitz T.A.
    Nature 376:362-366(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 22-239.

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: December 9, 2015
This is version 103 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.