| General information | | DisProt: | DP00722 | | Name: | Single-stranded DNA-binding protein | | Synonym(s): | SSB_ECO57
Helix-destabilizing protein
SSB
| | First appeared in release: | Release 6.00 (07/01/2012) | | UniProt: | P0AGE2 | | UniGene: | | | SwissProt: | SSB_ECO57 | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Escherichia coli O157:H7 | | Sequence length: | 178 | | Percent disordered: | 37% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MASRGVNKVI LVGNLGQDPE VRYMPNGGAV ANITLATSES WRDKATGEMK EQTEWHRVVL - 60
FGKLAEVASE YLRKGSQVYI EGQLRTRKWT DQSGQDRYTT EVVVNVGGTM QMLGGRQGGG - 120
APAGGNIGGG QPQGGWGQPQ QPQGGNQFSG GAQSRPQQSA PAAPSNEPPM DFDDDIPF
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| Functional narrative |
Function: This protein is essential for replication of the chromosomes and its single-stranded DNA phages. It is also involved in DNA recombination and repair.
SUBUNIT: Homotetramer.
PTM: Phosphorylated on tyrosine residue(s).
SIMILARITY: Contains 1 SSB domain.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Ordered | | Name: | DNA-binding domain (DBD) | | Location: | 1 - 113 | | Length: | 113 | | Region sequence: |
MASRGVNKVILVGNLGQDPEVRYMPNGGAVANITLATSESWRDKATGEMKEQTEWHRVVL
FGKLAEVASEYLRKGSQVYIEGQLRTRKWTDQSGQDRYTTEVVVNVGGTMQML | | Modification type: | Complex
| | PDB: | 1SRU:A | | Structural/functional type: | Function arises from the ordered state
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
- X-ray crystallography (293 K; pH: 7.5; SSB-dC(pC)34 complex 10 mg/mL; PEG4000 20 %; PEG200 20 %; Hepes 100 mM)
- Fluorescence polarization/anisotropy (298 K; pH: 8.1; (dA)35 or (dT)35; Hepes 10 mM; Na3EDTA 0.1 mM; NaCl 0.2 M; wtSSB or SSB{delta}C8) 0.14 uM)
| References:
- Savvides SN, Raghunathan S, Futterer K, Kozlov AG, Lohman TM, Waksman G. "The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA." Protein Sci. 2004; 13(7): 1942-7. PubMed: 15169953
| Comments:PDB structure 1SRU is from Savvides et al (2004).
Savvides et al describe the DNA-binding domain as well-ordered, forming the OB-fold common in ssDNA binding proteins.
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| Region 2 | | Type: | Disordered - Extended | | Name: | C-terminal domain (CTD) | | Location: | 114 - 178 | | Length: | 65 | | Region sequence: |
GGRQGGGAPAGGNIGGGQPQGGWGQPQQPQGGNQFSGGAQSRPQQSAPAAPSNEPPMDFD
DDIPF | | Modification type: | Complex
| | PDB: | 1SRU:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Protein inhibitor
Protein-protein binding
| Detection methods:
- X-ray crystallography (293 K; pH: 7.5; Hepes 100 mM; PEG200 20 %; PEG4000 20 %; SSB-dC(pC)34 complex 10 mg/mL)
- Fluorescence polarization/anisotropy (298 K; pH: 8.1; (dA)35 or (dT)35; Hepes 10 mM; Na3EDTA 0.1 mM; NaCl 0.2 M; wtSSB or SSB{delta}C8 0.014 uM)
| References:
- Fuxreiter M, Simon I, Bondos S. "Dynamic protein-DNA recognition: beyond what can be seen." Trends Biochem. Sci.. 2011; 36(8): 415-23. PubMed: 21620710
- Kozlov AG, Cox MM, Lohman TM. "Regulation of single-stranded DNA binding by the C termini of Escherichia coli single-stranded DNA-binding (SSB) protein." J. Biol. Chem.. 2010; 285(22): 17246-52. PubMed: 20360609
- Savvides SN, Raghunathan S, Futterer K, Kozlov AG, Lohman TM, Waksman G. "The C-terminal domain of full-length E. coli SSB is disordered even when bound to DNA." Protein Sci. 2004; 13(7): 1942-7. PubMed: 15169953
| Comments:PDB structure 1SRU is from Savvides et al (2004).
A discussion of the dynamic nature and flexibility modulation of SSB in a "fuzzy" protein-DNA complex is found in Fuxreiter et al (2011).
Kozlov et al (2010) describe the final nine residues of the C-terminal tail (aa M170-F178) as highly acidic and important for multiple protein-protein interactions, many of which are involved in DNA maintenance. Further, the disordered C-terminal tail inhibits ssDNA binding, possibly by intra-protein interaction with the ssDNA binding sites.
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| Comments |
AV sent 6-19-2012 (PMID:15169953)
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