ECOLI:SURA

Species (Taxon ID)	Escherichia coli (strain K12). (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	P0ABZ6
EMBL	U00096 AP009048 M68521 AB013134
PIR	E64726
RefSeq	NP_414595.1 YP_488359.1
PDB	1M5Y 2PV1 2PV2 2PV3
PDBsum	1M5Y 2PV1 2PV2 2PV3
ProteinModelPortal	P0ABZ6
SMR	P0ABZ6
DIP	DIP-35827N
IntAct	P0ABZ6
MINT	MINT-1242178
STRING	511145.b0053
SWISS-2DPAGE	P0ABZ6
PaxDb	P0ABZ6
PRIDE	P0ABZ6
EnsemblBacteria	AAC73164 BAB96620
GeneID	12932020 944812
KEGG	ecj:Y75_p0053 eco:b0053
PATRIC	32115205
EchoBASE	EB0978
EcoGene	EG10985
eggNOG	COG0760
HOGENOM	HOG000264337
InParanoid	P0ABZ6
KO	K03771
OMA	FGVHLIQ
OrthoDB	EOG6M9DS4
PhylomeDB	P0ABZ6
BioCyc	EcoCyc:EG10985-MONOMER ECOL316407:JW0052-MONOMER MetaCyc:EG10985-MONOMER
EvolutionaryTrace	P0ABZ6
PRO	PR:P0ABZ6
Proteomes	UP000000318 UP000000625
Genevestigator	P0ABZ6
GO	GO:0030288 GO:0042277 GO:0003755 GO:0051082 GO:0051085 GO:0043165 GO:0060274 GO:0006457 GO:0000413 GO:0050821
HAMAP	MF_01183
InterPro	IPR000297 IPR023058 IPR023034 IPR015391 IPR027304
Pfam	PF00639 PF09312
SUPFAM	SSF109998
PROSITE	PS01096 PS50198

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0050821	protein stabilization	PMID:21784935^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0060274	maintenance of stationary phase	PMID:2165476^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:8626309^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	PMID:8985185^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:8985185^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:8626309^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:8985185^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051085	chaperone cofactor-dependent protein refolding	PMID:17071751^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	PMID:11226178^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P02931 UniProtKB:P02932 UniProtKB:P02943	F	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:17071751^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:11226178^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	PMID:17908933^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P0AEU7	P	Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:17894549^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:17825319^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:15840585^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:14506253^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042277	peptide binding	PMID:11546789^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:24140104^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	PMID:15911532^[14]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:8985185^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:8626309^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:17908933^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	PMID:17071751^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:8985185^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003755	P	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003755	P	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003755	P	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003755	P	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003755	P	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0003755	P	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000297 InterPro:IPR023034	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	P	Seeded From UniProt	complete
part_of	GO:0030288	outer membrane-bounded periplasmic space	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	C	Seeded From UniProt	complete
enables	GO:0042277	peptide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	F	Seeded From UniProt	complete
involved_in	GO:0043165	Gram-negative-bacterium-type cell outer membrane assembly	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	P	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	P	Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	F	Seeded From UniProt	complete
involved_in	GO:0060274	maintenance of stationary phase	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023034	P	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:5.2.1.8	F	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000068663	P	Seeded From UniProt	complete
part_of	GO:0042597	periplasmic space	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000068663	C	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000068663	F	Seeded From UniProt	complete
	GO:0050821	protein stabilization	PMID:21784935^[1]	ECO:0000315			P	Fig.2	complete CACAO 7959
enables	GO:0051082	unfolded protein binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000068663	F	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0697	F	Seeded From UniProt	complete
part_of	GO:0042597	periplasmic space	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0574 UniProtKB-SubCell:SL-0200	C	Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F	Seeded From UniProt	complete
	GO:0044011	single-species biofilm formation on inanimate substrate	PMID:18180259^[15]	ECO:0000315			P		complete
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Notes

References

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

↑ ^1.0 ^1.1 Palomino, C et al. (2011) The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli. J. Bacteriol. 193 5222-30 PubMed GONUTS page
↑ Tormo, A et al. (1990) surA, an Escherichia coli gene essential for survival in stationary phase. J. Bacteriol. 172 4339-47 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Lazar, SW & Kolter, R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 178 1770-3 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 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 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
↑ ^6.0 ^6.1 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 GONUTS page
↑ ^7.0 ^7.1 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 GONUTS page
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ 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:21784935-1] 1.0 ^1.1 Palomino, C et al. (2011) The fimbrial usher FimD follows the SurA-BamB pathway for its assembly in the outer membrane of Escherichia coli. J. Bacteriol. 193 5222-30 PubMed GONUTS page

[PMID:2165476-2] 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:8626309-3] 3.0 ^3.1 ^3.2 Lazar, SW & Kolter, R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 178 1770-3 PubMed GONUTS page

[PMID:8985185-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 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:17071751-5] 5.0 ^5.1 ^5.2 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:11226178-6] 6.0 ^6.1 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 GONUTS page

[PMID:17908933-7] 7.0 ^7.1 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 GONUTS page

[PMID:17894549-8] 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:17825319-9] 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:15840585-10] 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:14506253-11] 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 GONUTS page

[PMID:11546789-12] 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:24140104-13] Han, MJ et al. (2014) Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains. J. Biosci. Bioeng. 117 437-42 PubMed GONUTS page

[PMID:15911532-14] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:18180259-15] 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 GONUTS page

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ECOLI:SURA

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