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Nomenclature

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Notes

Function

Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Notes

Localization

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Notes

Structure and Physical Properties

Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK LNAAQARQQL
PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI ANIAKQNNMT LDQMRSRLAY
DGLNYNTYRN QIRKEMIISE VRNNEVRRRI TILPQEVESL AQQVGNQNDA STELNLSHIL
IPLPENPTSD QVNEAESQAR AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP
GIFAQALSTA KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD
EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD PAFRDALTRL
NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM LMNRKFSEEA ASWMQEQRAS
AYVKILSN

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki. Type Residues Description Notes References motif 1-20 UniProt Manual:Signal Peptides UniProt:P0ABZ6 edit table

Notes

Gene Product Resources

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Notes

Accessions in Other Databases

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Notes

Links

References

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1. ↑ ^{1.0 1.1 1.2 1.3 1.4} Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
2. ↑ ^{2.0 2.1 2.2} EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
3. ↑ ^{3.0 3.1} EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
5. ↑ ^{5.0 5.1 5.2 5.3} EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
6. ↑ ^{6.0 6.1 6.2 6.3 6.4 6.5 6.6} EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
7. ↑ ^{7.0 7.1} Behrens S et al. (2001) The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J 20: 285-94 PubMed EcoliWiki page
8. ↑ ^{8.0 8.1} Sklar JG et al. (2007) Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli. Genes Dev 21: 2473-84 PubMed EcoliWiki page
9. ↑ Vuong P et al. (2008) Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J Bacteriol 190: 1507-17 PubMed EcoliWiki page
10. ↑ Webb HM et al. (2001) Interaction of the periplasmic peptidylprolyl cis-trans isomerase SurA with model peptides. The N-terminal region of SurA id essential and sufficient for peptide binding. J Biol Chem 276: 45622-7 PubMed EcoliWiki page
11. ↑ Bitto E & McKay DB (2003) The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. J Biol Chem 278: 49316-22 PubMed EcoliWiki page
12. ↑ Hennecke G et al. (2005) The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J Biol Chem 280: 23540-8 PubMed EcoliWiki page
13. ↑ Xu X et al. (2007) The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J Mol Biol 373: 367-81 PubMed EcoliWiki page
14. ↑ Alcock FH et al. (2008) Conserved substrate binding by chaperones in the bacterial periplasm and the mitochondrial intermembrane space. Biochem J 409: 377-87 PubMed EcoliWiki page
15. ↑ Niba ET et al. (2007) A genome-wide approach to identify the genes involved in biofilm formation in E. coli. DNA Res 14: 237-46 PubMed EcoliWiki page
16. ↑ ^{16.0 16.1} Ureta AR et al. (2007) Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment. J Bacteriol 189: 446-54 PubMed EcoliWiki page
17. ↑ Tormo A et al. (1990) surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339-47 PubMed EcoliWiki page
18. ↑ ^{18.0 18.1} Lazar SW & Kolter R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770-3 PubMed EcoliWiki page
19. ↑ ^{19.0 19.1 19.2} Rouvière PE & Gross CA (1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev 10: 3170-82 PubMed EcoliWiki page
20. ↑ ^{20.0 20.1} Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page
21. ↑ ^{21.0 21.1 21.2 21.3 21.4 21.5} Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
22. ↑ Link AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18: 1259-313 PubMed EcoliWiki page

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