ECOLI:SURA

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Species (Taxon ID)	Escherichia coli (strain K12). (taxon:83333)
Gene Name(s)	surA
Protein Name(s)	Chaperone surA Peptidyl-prolyl cis-trans isomerase surA PPIase surA Rotamase surA Survival protein A
External Links
UniProt Identifier	SURA_ECOLI
UniProt Accessions	P0ABZ6, P21202, P75630, Q8KIP6, Q8KMY0,
EMBL	U00096, AP009048, M68521, AB013134,
PIR	E64726,
RefSeq	AP_000717.1, NP_414595.1,
PDB	1M5Y, 2PV1, 2PV2, 2PV3,
Pfam	PF00639, PF09312,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect
	GO:0060274	maintenance of stationary phase	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0042277	peptide binding	PMID:17894549^[1]	IDA: Inferred from Direct Assay		F
	GO:0051082	unfolded protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02943	F
	GO:0042597	periplasmic space	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0200	C
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	F
	GO:0050821	protein stabilization	PMID:17071751^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0050821	protein stabilization	PMID:11226178^[2]	IDA: Inferred from Direct Assay		P
	GO:0006457	protein folding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	P
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:8985185^[4]	IDA: Inferred from Direct Assay		F
	GO:0006457	protein folding	PMID:17071751^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0006457	protein folding	PMID:8626309^[5]	IMP: Inferred from Mutant Phenotype		P
	GO:0030288	outer membrane-bounded periplasmic space	PMID:8985185^[4]	IDA: Inferred from Direct Assay		C
	GO:0042710	biofilm formation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0006457	protein folding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0051082	unfolded protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02932	F
	GO:0042277	peptide binding	PMID:14506253^[6]	IDA: Inferred from Direct Assay		F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:5.2.1.8	F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	F
	GO:0051082	unfolded protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02932	F
	GO:0042277	peptide binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	F
	GO:0051082	unfolded protein binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	F
	GO:0006457	protein folding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008880	P
	GO:0005515	protein binding	PMID:17908933^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P0A940	F
	GO:0006457	protein folding	PMID:17908933^[7]	IMP: Inferred from Mutant Phenotype		P
	GO:0015031	protein transport	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008880	P
	GO:0060274	maintenance of stationary phase	PMID:2165476^[8]	IMP: Inferred from Mutant Phenotype		P
	GO:0050821	protein stabilization	PMID:8626309^[5]	IMP: Inferred from Mutant Phenotype		P
	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0051085	chaperone mediated protein folding requiring cofactor	PMID:17071751^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0042277	peptide binding	PMID:17825319^[9]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:18165306^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P0A940	F
	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	PMID:17908933^[7]	IGI: Inferred from Genetic Interaction		P
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:8985185^[4]	IDA: Inferred from Direct Assay		F
	GO:0016853	isomerase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000297	F
	GO:0030288	outer membrane-bounded periplasmic space	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	C
	GO:0016853	isomerase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0413	F
	GO:0051082	unfolded protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02931	F
	GO:0042277	peptide binding	PMID:15840585^[11]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02932	F
	GO:0042710	biofilm formation	PMID:18180259^[12]	IMP: Inferred from Mutant Phenotype		P
	GO:0051082	unfolded protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02931	F
	GO:0050821	protein stabilization	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0051085	chaperone mediated protein folding requiring cofactor	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0006457	protein folding	PMID:8626309^[5]	IMP: Inferred from Mutant Phenotype		P
	GO:0051082	unfolded protein binding	PMID:11226178^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P02943	F
	GO:0042597	periplasmic space	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0574	C
	GO:0042277	peptide binding	PMID:11546789^[13]	IDA: Inferred from Direct Assay		F
	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	PMID:8985185^[4]	IMP: Inferred from Mutant Phenotype		P
	GO:0006457	protein folding	PMID:8985185^[4]	IMP: Inferred from Mutant Phenotype		P
	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:5.2.1.8	P
	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	P
	GO:0000413	protein peptidyl-prolyl isomerization	PMID:8985185^[4]	IDA: Inferred from Direct Assay		P
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:5.2.1.8	F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:8985185^[4]	IDA: Inferred from Direct Assay		F
	GO:0006457	protein folding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008880	P
	GO:0006457	protein folding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0006457	protein folding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	P
	GO:0006457	protein folding	PMID:17071751^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0006457	protein folding	PMID:17908933^[7]	IMP: Inferred from Mutant Phenotype		P
	GO:0006457	protein folding	PMID:8626309^[5]	IMP: Inferred from Mutant Phenotype		P
	GO:0006457	protein folding	PMID:8985185^[4]	IMP: Inferred from Mutant Phenotype		P
	GO:0015031	protein transport	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008880	P
	GO:0016853	isomerase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000297	F
	GO:0016853	isomerase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0413	F
	GO:0030288	outer membrane-bounded periplasmic space	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	C
	GO:0030288	outer membrane-bounded periplasmic space	PMID:8985185^[4]	IDA: Inferred from Direct Assay		C
	GO:0042277	peptide binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	F
	GO:0042277	peptide binding	PMID:11546789^[13]	IDA: Inferred from Direct Assay		F
	GO:0042277	peptide binding	PMID:14506253^[6]	IDA: Inferred from Direct Assay		F
	GO:0042277	peptide binding	PMID:15840585^[11]	IDA: Inferred from Direct Assay		F
	GO:0042277	peptide binding	PMID:17825319^[9]	IDA: Inferred from Direct Assay		F
	GO:0042277	peptide binding	PMID:17894549^[1]	IDA: Inferred from Direct Assay		F
	GO:0042597	periplasmic space	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0574	C
	GO:0042597	periplasmic space	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0200	C
	GO:0042710	biofilm formation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0042710	biofilm formation	PMID:18180259^[12]	IMP: Inferred from Mutant Phenotype		P
	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	PMID:8985185^[4]	IMP: Inferred from Mutant Phenotype		P
	GO:0050821	protein stabilization	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0050821	protein stabilization	PMID:11226178^[2]	IDA: Inferred from Direct Assay		P
	GO:0050821	protein stabilization	PMID:17071751^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0050821	protein stabilization	PMID:8626309^[5]	IMP: Inferred from Mutant Phenotype		P
	GO:0051082	unfolded protein binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	F
	GO:0051085	chaperone mediated protein folding requiring cofactor	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0051085	chaperone mediated protein folding requiring cofactor	PMID:17071751^[3]	IMP: Inferred from Mutant Phenotype		P
	GO:0060274	maintenance of stationary phase	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR023034	P
	GO:0060274	maintenance of stationary phase	PMID:2165476^[8]	IMP: Inferred from Mutant Phenotype		P
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 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 GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 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 GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 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 GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 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 GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 Lazar SW & Kolter R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770-3 PubMed GONUTS page
↑ ^6.0 ^6.1 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 GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 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 GONUTS page
↑ ^8.0 ^8.1 Tormo A et al. (1990) surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339-47 PubMed GONUTS page
↑ ^9.0 ^9.1 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 GONUTS page
↑ Vuong P et al. (2008) Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J Bacteriol 190: 1507-17 PubMed GONUTS page
↑ ^11.0 ^11.1 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 GONUTS page
↑ ^12.0 ^12.1 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 GONUTS page
↑ ^13.0 ^13.1 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 GONUTS page

[PMID:17894549-0] 1.0 ^1.1 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 GONUTS page

[PMID:11226178-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 ^2.7 ^2.8 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 GONUTS page

[PMID:17071751-2] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 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 GONUTS page

[PMID:8985185-3] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 ^4.7 ^4.8 ^4.9 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 GONUTS page

[PMID:8626309-4] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 Lazar SW & Kolter R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770-3 PubMed GONUTS page

[PMID:14506253-5] 6.0 ^6.1 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 GONUTS page

[PMID:17908933-6] 7.0 ^7.1 ^7.2 ^7.3 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 GONUTS page

[PMID:2165476-7] 8.0 ^8.1 Tormo A et al. (1990) surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339-47 PubMed GONUTS page

[PMID:17825319-8] 9.0 ^9.1 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 GONUTS page

[PMID:18165306-9] Vuong P et al. (2008) Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J Bacteriol 190: 1507-17 PubMed GONUTS page

[PMID:15840585-10] 11.0 ^11.1 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 GONUTS page

[PMID:18180259-11] 12.0 ^12.1 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 GONUTS page

[PMID:11546789-12] 13.0 ^13.1 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 GONUTS page

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ECOLI:SURA

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