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Protein

Single-stranded DNA-binding protein

Gene

ssb

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism. Acts as a sliding platform that migrates on DNA via reptation.UniRule annotation3 Publications

Enzyme regulationi

The C-terminal tail exerts an inhibitory effect on ssDNA binding.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi55 – 61UniRule annotation7

GO - Molecular functioni

  • enzyme activator activity Source: UniProtKB
  • identical protein binding Source: EcoCyc
  • single-stranded DNA binding Source: EcoCyc

GO - Biological processi

  • DNA replication Source: UniProtKB-KW
  • mismatch repair Source: EcoCyc
  • positive regulation of catalytic activity Source: UniProtKB
  • recombinational repair Source: EcoCyc
  • SOS response Source: EcoCyc

Keywordsi

Molecular functionDNA-binding
Biological processDNA damage, DNA recombination, DNA repair, DNA replication

Enzyme and pathway databases

BioCyciEcoCyc:EG10976-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Single-stranded DNA-binding proteinUniRule annotation
Short name:
SSBUniRule annotation
Alternative name(s):
Helix-destabilizing protein
Gene namesi
Name:ssb
Synonyms:exrB, lexC
Ordered Locus Names:b4059, JW4020
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10976. ssb.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5G → D: Increased frequency of precise excision of transposon Tn10 derivatives (mutant SSB-200). 1 Publication1
Mutagenesisi11L → F: Increased frequency of precise excision of transposon Tn10 derivatives (mutant SSB-202). 1 Publication1
Mutagenesisi25P → S: Increased frequency of precise excision of transposon Tn10 derivatives (mutant SSB-202). 1 Publication1
Mutagenesisi56H → L: Reduces DNA-binding affinity. 1 Publication1
Mutagenesisi56H → Y: Destabilizes the tetramer (mutant SSB-1). 1 Publication1
Mutagenesisi61F → A: Reduces DNA-binding affinity. 1 Publication1
Mutagenesisi103V → M: Increased frequency of precise excision of transposon Tn10 derivatives (mutant SSB-201). 1 Publication1
Mutagenesisi177P → S: Strongly reduced exonuclease I (sbcB) stimulation. 1 Publication1

Chemistry databases

DrugBankiDB04243. 5-Methyluridine 5'-Monophosphate.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000960362 – 178Single-stranded DNA-binding proteinAdd BLAST177

Post-translational modificationi

Phosphorylated on tyrosine residue(s).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0AGE0.
PRIDEiP0AGE0.

2D gel databases

SWISS-2DPAGEiP0AGE0.

Interactioni

Subunit structurei

Homotetramer. Interacts, via its C-terminus, with several proteins involved in DNA metabolism such as DnaG, HolC, PriA, PriB, RecO, RecQ and SbcB.UniRule annotation11 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262671. 106 interactors.
DIPiDIP-35980N.
IntActiP0AGE0. 12 interactors.
MINTiMINT-8298796.
STRINGi316385.ECDH10B_4248.

Structurei

Secondary structure

1178
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 17Combined sources12
Beta strandi20 – 22Combined sources3
Beta strandi25 – 27Combined sources3
Beta strandi30 – 37Combined sources8
Beta strandi45 – 48Combined sources4
Beta strandi54 – 61Combined sources8
Helixi63 – 71Combined sources9
Beta strandi77 – 89Combined sources13
Beta strandi91 – 94Combined sources4
Beta strandi96 – 103Combined sources8
Beta strandi105 – 107Combined sources3
Beta strandi108 – 111Combined sources4
Beta strandi120 – 124Combined sources5
Beta strandi136 – 139Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EQQX-ray3.20A/B/C/D1-178[»]
1EYGX-ray2.80A/B/C/D1-116[»]
1KAWX-ray2.90A/B/C/D2-136[»]
1QVCX-ray2.20A/B/C/D2-146[»]
1SRUX-ray3.30A/B/C/D1-113[»]
3C94X-ray2.70B/C170-178[»]
3SXUX-ray1.85C175-178[»]
3UF7X-ray1.20B/C170-178[»]
4MZ9X-ray2.20A/B/C/D1-178[»]
4Z0UX-ray2.00D/E170-178[»]
ProteinModelPortaliP0AGE0.
SMRiP0AGE0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AGE0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 111SSBUniRule annotationAdd BLAST106

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi173 – 178Important for interaction with partner proteins6

Phylogenomic databases

eggNOGiENOG4108UUM. Bacteria.
COG0629. LUCA.
HOGENOMiHOG000106483.
InParanoidiP0AGE0.
KOiK03111.
PhylomeDBiP0AGE0.

Family and domain databases

CDDicd04496. SSB_OBF. 1 hit.
HAMAPiMF_00984. SSB. 1 hit.
InterProiView protein in InterPro
IPR012340. NA-bd_OB-fold.
IPR000424. Primosome_PriB/ssb.
IPR011344. ssDNA-bd.
PANTHERiPTHR10302:SF16. PTHR10302:SF16. 1 hit.
PfamiView protein in Pfam
PF00436. SSB. 1 hit.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00621. ssb. 1 hit.
PROSITEiView protein in PROSITE
PS50935. SSB. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AGE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASRGVNKVI LVGNLGQDPE VRYMPNGGAV ANITLATSES WRDKATGEMK
60 70 80 90 100
EQTEWHRVVL FGKLAEVASE YLRKGSQVYI EGQLRTRKWT DQSGQDRYTT
110 120 130 140 150
EVVVNVGGTM QMLGGRQGGG APAGGNIGGG QPQGGWGQPQ QPQGGNQFSG
160 170
GAQSRPQQSA PAAPSNEPPM DFDDDIPF
Length:178
Mass (Da):18,975
Last modified:January 23, 2007 - v2
Checksum:iF0AF43B6DC8D02FC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121A → AQ no nucleotide entry (PubMed:6351061).Curated1
Sequence conflicti134G → S in AAA24649 (PubMed:6270666).Curated1
Sequence conflicti171D → DG no nucleotide entry (PubMed:6351061).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01704 Genomic DNA. Translation: AAA24649.1.
U00006 Genomic DNA. Translation: AAC43153.1.
U00096 Genomic DNA. Translation: AAC77029.1.
AP009048 Genomic DNA. Translation: BAE78061.1.
PIRiB65214. DDEC.
RefSeqiNP_418483.1. NC_000913.3.
WP_000168305.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77029; AAC77029; b4059.
BAE78061; BAE78061; BAE78061.
GeneIDi948570.
KEGGiecj:JW4020.
eco:b4059.
PATRICifig|511145.12.peg.4180.

Similar proteinsi

Entry informationi

Entry nameiSSB_ECOLI
AccessioniPrimary (citable) accession number: P0AGE0
Secondary accession number(s): P02339, Q2M6P5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 105 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references