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P0ABZ6 (SURA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone SurA
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase SurA
Short name=PPIase SurA
EC=5.2.1.8
Rotamase SurA
Survival protein A
Gene names
Name:surA
Ordered Locus Names:b0053, JW0052
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length428 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12 Ref.13 Ref.16

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0). HAMAP-Rule MF_01183

Subcellular location

Periplasm. Note: Is capable of associating with the outer membrane. HAMAP-Rule MF_01183

Domain

The PPIase activity resides only in the second parvulin domain. The N-terminal region and the C-terminal tail are necessary and sufficient for the chaperone activity of SurA. The PPIase activity is dispensable for SurA function as a SurA protein with a deletion of the parvulin domains is almost completely functional in vivo. The N-terminal region and the C-terminal tail are also required for porin recognition. Ref.13

Sequence similarities

Contains 2 PpiC domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

bamBP777742EBI-558651,EBI-907297

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.7 Ref.8 Ref.9
Chain21 – 428408Chaperone SurA HAMAP-Rule MF_01183
PRO_0000025542

Regions

Domain171 – 272102PpiC 1
Domain282 – 382101PpiC 2

Experimental info

Sequence conflict251V → D Ref.1
Sequence conflict1161S → T Ref.1
Sequence conflict2131G → GFG Ref.1

Secondary structure

.......................................................... 428
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABZ6 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 25F6AD4B903CBD8E

FASTA42847,284
        10         20         30         40         50         60 
MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK LNAAQARQQL 

        70         80         90        100        110        120 
PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI ANIAKQNNMT LDQMRSRLAY 

       130        140        150        160        170        180 
DGLNYNTYRN QIRKEMIISE VRNNEVRRRI TILPQEVESL AQQVGNQNDA STELNLSHIL 

       190        200        210        220        230        240 
IPLPENPTSD QVNEAESQAR AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP 

       250        260        270        280        290        300 
GIFAQALSTA KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD 

       310        320        330        340        350        360 
EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD PAFRDALTRL 

       370        380        390        400        410        420 
NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM LMNRKFSEEA ASWMQEQRAS 


AYVKILSN 

« Hide

References

« Hide 'large scale' references
[1]Almiron M., Tormo A., Kolter R.
Unpublished observations (JAN-1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12.
[3]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 331-428.
Strain: K12.
[6]"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.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-32.
Strain: K12 / EMG2.
[8]"SurA assists the folding of Escherichia coli outer membrane proteins."
Lazar S.W., Kolter R.
J. Bacteriol. 178:1770-1773(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-30, CHARACTERIZATION.
[9]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 21-24.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[10]"surA, an Escherichia coli gene essential for survival in stationary phase."
Tormo A., Almiron M., Kolter R.
J. Bacteriol. 172:4339-4347(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[12]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN FUNCTION.
[14]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE RECOGNITION.
[15]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE RECOGNITION.
[16]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN PILUS BIOGENESIS.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[17]"Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins."
Bitto E., McKay D.B.
Structure 10:1489-1498(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-428.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00096 Genomic DNA. Translation: AAC73164.1.
AP009048 Genomic DNA. Translation: BAB96620.2.
M68521 Genomic DNA. Translation: AAA24304.1.
AB013134 Genomic DNA. Translation: BAA34131.1.
PIRE64726.
RefSeqNP_414595.1. NC_000913.3.
YP_488359.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M5YX-ray3.00A/B/C/D21-428[»]
2PV1X-ray1.30A172-274[»]
2PV2X-ray1.30A/B/C/D172-274[»]
2PV3X-ray3.39A/B21-428[»]
ProteinModelPortalP0ABZ6.
SMRP0ABZ6. Positions 25-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35827N.
IntActP0ABZ6. 10 interactions.
MINTMINT-1242178.
STRING511145.b0053.

2D gel databases

SWISS-2DPAGEP0ABZ6.

Proteomic databases

PaxDbP0ABZ6.
PRIDEP0ABZ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73164; AAC73164; b0053.
BAB96620; BAB96620; BAB96620.
GeneID12932020.
944812.
KEGGecj:Y75_p0053.
eco:b0053.
PATRIC32115205. VBIEscCol129921_0054.

Organism-specific databases

EchoBASEEB0978.
EcoGeneEG10985. surA.

Phylogenomic databases

eggNOGCOG0760.
HOGENOMHOG000264337.
KOK03771.
OMAFGVHLIQ.
OrthoDBEOG6M9DS4.
PhylomeDBP0ABZ6.
ProtClustDBPRK10770.

Enzyme and pathway databases

BioCycEcoCyc:EG10985-MONOMER.
ECOL316407:JW0052-MONOMER.
MetaCyc:EG10985-MONOMER.

Gene expression databases

GenevestigatorP0ABZ6.

Family and domain databases

HAMAPMF_01183. Chaperone_SurA.
InterProIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR023034. PPIase_SurA.
IPR015391. SurA_N.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamPF00639. Rotamase. 2 hits.
PF09312. SurA_N. 1 hit.
[Graphical view]
SUPFAMSSF109998. SSF109998. 1 hit.
PROSITEPS01096. PPIC_PPIASE_1. 2 hits.
PS50198. PPIC_PPIASE_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABZ6.
PROP0ABZ6.

Entry information

Entry nameSURA_ECOLI
AccessionPrimary (citable) accession number: P0ABZ6
Secondary accession number(s): P21202 expand/collapse secondary AC list , P75630, Q8KIP6, Q8KMY0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: April 16, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene