Difference between revisions of "SsbA"
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ssbA_4198886_4199404_-1 ssbA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ssbA_4198886_4199404_-1 ssbA] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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<pubmed> 22976189 </pubmed> | <pubmed> 22976189 </pubmed> | ||
== Original publications == | == Original publications == | ||
− | + | <pubmed>17853894,19730681 11948146,16479537,11948165 16549871 20122408 14762004 20581116 22054219 22373918 22517742 21859751, 21170359, 21958350,23268446 23536821</pubmed> | |
− | <pubmed>17853894,19730681 11948146,16479537,11948165 16549871 20122408 14762004 20581116 22054219 22373918 22517742 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 13:34, 29 March 2013
- Description: single-strand DNA-binding protein, part of the replisome
Gene name | ssbA |
Synonyms | ssb |
Essential | yes PubMed |
Product | single-strand DNA-binding protein |
Function | DNA replication, DNA repair/ recombination |
Gene expression levels in SubtiExpress: ssbA | |
Interactions involving this protein in SubtInteract: SsbA | |
MW, pI | 18 kDa, 4.822 |
Gene length, protein length | 516 bp, 172 aa |
Immediate neighbours | rpsR, rpsF |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
DNA replication, DNA repair/ recombination, essential genes, phosphoproteins
This gene is a member of the following regulons
ComK regulon, stringent response
The gene
Basic information
- Locus tag: BSU40900
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s): SsbB
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: Phosphorylation of Ssb increases binding to single-stranded DNA in vitro almost 200-fold PubMed
- Interactions:
- forms tetramers PubMed
- part of the replisome: PolC-HolA-HolB-DnaX-DnaN-DnaG-DnaC-DnaI-DnaD-SsbA-DnaE-PriA-DnaB PubMed
- SsbA-SbcC PubMed
- SsbA-RecG PubMed
- SsbA-YrvE PubMed
- SsbA-YrvN PubMed
- SsbA (bound to ssDNA) -RecO, this helps to dislodge SsbA and SsbB from ssDNA PubMed
- SsbA-YqiB PubMed
- SsbA-Ung PubMed
- SsbA-YpbB PubMed
- SsbA-YrrC PubMed
- DnaE-DnaN PubMed
Database entries
- UniProt: P37455
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Dusica Vujaklija, Boris Macek
Detecting posttranslational modifications of bacterial SSB proteins.
Methods Mol Biol: 2012, 922;205-18
[PubMed:22976189]
[WorldCat.org]
[DOI]
(I p)
Original publications
Aimee H Marceau, Douglas A Bernstein, Brian W Walsh, Walker Shapiro, Lyle A Simmons, James L Keck
Protein interactions in genome maintenance as novel antibacterial targets.
PLoS One: 2013, 8(3);e58765
[PubMed:23536821]
[WorldCat.org]
[DOI]
(I p)
Elena M Seco, John C Zinder, Carol M Manhart, Ambra Lo Piano, Charles S McHenry, Silvia Ayora
Bacteriophage SPP1 DNA replication strategies promote viral and disable host replication in vitro.
Nucleic Acids Res: 2013, 41(3);1711-21
[PubMed:23268446]
[WorldCat.org]
[DOI]
(I p)
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Tribhuwan Yadav, Begoña Carrasco, Angela R Myers, Nicholas P George, James L Keck, Juan C Alonso
Genetic recombination in Bacillus subtilis: a division of labor between two single-strand DNA-binding proteins.
Nucleic Acids Res: 2012, 40(12);5546-59
[PubMed:22373918]
[WorldCat.org]
[DOI]
(I p)
Wei Zhang, Xiujuan Lü, Wenke Zhang, Jiacong Shen
EMSA and single-molecule force spectroscopy study of interactions between Bacillus subtilis single-stranded DNA-binding protein and single-stranded DNA.
Langmuir: 2011, 27(24);15008-15
[PubMed:22054219]
[WorldCat.org]
[DOI]
(I p)
Andrew D Klocko, Jeremy W Schroeder, Brian W Walsh, Justin S Lenhart, Margery L Evans, Lyle A Simmons
Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork.
Mol Microbiol: 2011, 82(3);648-63
[PubMed:21958350]
[WorldCat.org]
[DOI]
(I p)
Paula P Cardenas, Thomas Carzaniga, Sandro Zangrossi, Federica Briani, Esther Garcia-Tirado, Gianni Dehò, Juan C Alonso
Polynucleotide phosphorylase exonuclease and polymerase activities on single-stranded DNA ends are modulated by RecN, SsbA and RecA proteins.
Nucleic Acids Res: 2011, 39(21);9250-61
[PubMed:21859751]
[WorldCat.org]
[DOI]
(I p)
Audrey Costes, François Lecointe, Stephen McGovern, Sophie Quevillon-Cheruel, Patrice Polard
The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks.
PLoS Genet: 2010, 6(12);e1001238
[PubMed:21170359]
[WorldCat.org]
[DOI]
(I e)
Candela Manfredi, Yuki Suzuki, Tribhuwan Yadav, Kunio Takeyasu, Juan C Alonso
RecO-mediated DNA homology search and annealing is facilitated by SsbA.
Nucleic Acids Res: 2010, 38(20);6920-9
[PubMed:20581116]
[WorldCat.org]
[DOI]
(I p)
Glenn M Sanders, H Garry Dallmann, Charles S McHenry
Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases.
Mol Cell: 2010, 37(2);273-81
[PubMed:20122408]
[WorldCat.org]
[DOI]
(I p)
Dawit Kidane, Begoña Carrasco, Candela Manfredi, Katharina Rothmaier, Silvia Ayora, Serkalem Tadesse, Juan C Alonso, Peter L Graumann
Evidence for different pathways during horizontal gene transfer in competent Bacillus subtilis cells.
PLoS Genet: 2009, 5(9);e1000630
[PubMed:19730681]
[WorldCat.org]
[DOI]
(I p)
François Lecointe, Céline Sérèna, Marion Velten, Audrey Costes, Stephen McGovern, Jean-Christophe Meile, Jeffrey Errington, S Dusko Ehrlich, Philippe Noirot, Patrice Polard
Anticipating chromosomal replication fork arrest: SSB targets repair DNA helicases to active forks.
EMBO J: 2007, 26(19);4239-51
[PubMed:17853894]
[WorldCat.org]
[DOI]
(P p)
Ivan Mijakovic, Dina Petranovic, Boris Macek, Tina Cepo, Matthias Mann, Julian Davies, Peter R Jensen, Dusica Vujaklija
Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine.
Nucleic Acids Res: 2006, 34(5);1588-96
[PubMed:16549871]
[WorldCat.org]
[DOI]
(I e)
Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537]
[WorldCat.org]
[DOI]
(P p)
Cordula Lindner, Reindert Nijland, Mariska van Hartskamp, Sierd Bron, Leendert W Hamoen, Oscar P Kuipers
Differential expression of two paralogous genes of Bacillus subtilis encoding single-stranded DNA binding protein.
J Bacteriol: 2004, 186(4);1097-105
[PubMed:14762004]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165]
[WorldCat.org]
[DOI]
(P p)
Mitsuo Ogura, Hirotake Yamaguchi, Kazuo Kobayashi, Naotake Ogasawara, Yasutaro Fujita, Teruo Tanaka
Whole-genome analysis of genes regulated by the Bacillus subtilis competence transcription factor ComK.
J Bacteriol: 2002, 184(9);2344-51
[PubMed:11948146]
[WorldCat.org]
[DOI]
(P p)