Chaperone SurA Recombinant Protein | surA recombinant protein

Recombinant Escherichia coli Chaperone SurA

Cat. Num. AAA1142522

• Gene Names: surA; ECK0054; JW0052
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Chaperone SurA; Recombinant Escherichia coli Chaperone SurA; Peptidyl-prolyl cis-trans isomerase SurA (EC:5.2.1.8); PPIase SurA; Rotamase SurA; Survival protein A; surA recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 21-428aa; Full Length
• Sequence: APQVVDKVAAVVNNGVVLESDVDGLMQSVKLNAAQARQQLPDDATLRHQIMERLIMDQIILQMGQKMGVKISDEQLDQAIANIAKQNNMTLDQMRSRLAYDGLNYNTYRNQIRKEMIISEVRNNEVRRRITILPQEVESLAQQVGNQNDASTELNLSHILIPLPENPTSDQVNEAESQARAIVDQARNGADFGKLAIAHSADQQALNGGQMGWGRIQELPGIFAQALSTAKKGDIVGPIRSGVGFHILKVNDLRGESKNISVTEVHARHILLKPSPIMTDEQARVKLEQIAADIKSGKTTFAAAAKEFSQDPGSANQGGDLGWATPDIFDPAFRDALTRLNKGQMSAPVHSSFGWHLIELLDTRNVDKTDAAQKDRAYRMLMNRKFSEEAASWMQEQRASAYVKILSN
• Sequence Length: 428

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for surA recombinant protein

Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E Coli in stationary phase. Required for pilus biogenesis.

References

Almiron M., Tormo A., Kolter R.Unpublished observations (JAN-1993) Systematic sequencing of the Escherichia coli genome analysis of the 0-2.4 min region.Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.Nucleic Acids Res. 20:3305-3308(1992) The complete genome sequence of Escherichia coli K-12.Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.Science 277:1453-1462(1997) Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.Mol. Syst. Biol. 2:E1-E5(2006) Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12.Roa B.B., Connolly D.M., Winkler M.E.J. Bacteriol. 171:4767-4777(1989) N-hexane sensitivity of Escherichia coli due to low expression of ostA/imp by insertion of IS2 and identification of the gene product as an outer membrane protein.Abe S., Okutsu T., Negishi T., Nakajima H., Aono R.Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.Link A.J., Robison K., Church G.M.Electrophoresis 18:1259-1313(1997) SurA assists the folding of Escherichia coli outer membrane proteins.Lazar S.W., Kolter R.J. Bacteriol. 178:1770-1773(1996) Protein identification with N and C-terminal sequence tags in proteome projects.Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.J. Mol. Biol. 278:599-608(1998) surA, an Escherichia coli gene essential for survival in stationary phase.Tormo A., Almiron M., Kolter R.J. Bacteriol. 172:4339-4347(1990) New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH.Missiakas D., Betton J.-M., Raina S.Mol. Microbiol. 21:871-884(1996) SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins.Rouviere P.E., Gross C.A.Genes Dev. 10:3170-3182(1996) The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.Behrens S., Maier R., de Cock H., Schmid F.X., Gross C.A.EMBO J. 20:285-294(2001) The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins.Bitto E., McKay D.B.J. Biol. Chem. 278:49316-49322(2003) The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition.Hennecke G., Nolte J., Volkmer-Engert R., Schneider-Mergener J., Behrens S.J. Biol. Chem. 280:23540-23548(2005) Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli.Justice S.S., Hunstad D.A., Harper J.R., Duguay A.R., Pinkner J.S., Bann J., Frieden C., Silhavy T.J., Hultgren S.J.J. Bacteriol. 187:7680-7686(2005) Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.Bitto E., McKay D.B.Structure 10:1489-1498(2002)

NCBI and Uniprot Product Information

• NCBI GI #: 16128047
• NCBI GeneID: 944812
• NCBI Accession #: NP_414595.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P0ABZ6; P21202; P75630; Q8KIP6; Q8KMY0
• Molecular Weight: 47.1 kDa
• NCBI Official Full Name: peptidyl-prolyl cis-trans isomerase (PPIase)
• NCBI Official Symbol: surA
• NCBI Official Synonym Symbols: ECK0054; JW0052
• NCBI Protein Information: peptidyl-prolyl cis-trans isomerase (PPIase)
• UniProt Protein Name: Chaperone SurA
• Protein Family: Chaperone
• UniProt Gene Name: surA
• UniProt Synonym Gene Names: PPIase SurA
• UniProt Entry Name: SURA_ECOLI

NCBI Description

Parvulin (ppiC) family. [More information is available at EcoGene: EG10985]. SurA in Escherichia coli is a periplasmic peptidyl-prolyl isomerase which is necessary for the proper folding of outer membrane proteins including OmpA, OmpF and LamB. [More information is available at EcoCyc: EG10985].

Uniprot Description

Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.