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P0ABZ6

- SURA_ECOLI

UniProt

P0ABZ6 - SURA_ECOLI

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Protein
Chaperone SurA
Gene
surA, b0053, JW0052
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).UniRule annotation

GO - Molecular functioni

  1. peptide binding Source: EcoCyc
  2. peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
  3. protein binding Source: IntAct
  4. unfolded protein binding Source: EcoCyc
Complete GO annotation...

GO - Biological processi

  1. Gram-negative-bacterium-type cell outer membrane assembly Source: EcoliWiki
  2. biofilm formation Source: EcoCyc
  3. chaperone mediated protein folding requiring cofactor Source: EcoCyc
  4. maintenance of stationary phase Source: EcoliWiki
  5. protein folding Source: EcoCyc
  6. protein peptidyl-prolyl isomerization Source: GOC
  7. protein stabilization Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase, Rotamase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone SurA
Alternative name(s):
Peptidyl-prolyl cis-trans isomerase SurA (EC:5.2.1.8)
Short name:
PPIase SurA
Rotamase SurA
Survival protein A
Gene namesi
Name:surA
Ordered Locus Names:b0053, JW0052
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10985. surA.

Subcellular locationi

Periplasm
Note: Is capable of associating with the outer membrane.UniRule annotation

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20203 Publications
Add
BLAST
Chaini21 – 428408Chaperone SurAUniRule annotation
PRO_0000025542Add
BLAST

Proteomic databases

PaxDbiP0ABZ6.
PRIDEiP0ABZ6.

2D gel databases

SWISS-2DPAGEiP0ABZ6.

Expressioni

Gene expression databases

GenevestigatoriP0ABZ6.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
bamBP777742EBI-558651,EBI-907297

Protein-protein interaction databases

DIPiDIP-35827N.
IntActiP0ABZ6. 10 interactions.
MINTiMINT-1242178.
STRINGi511145.b0053.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 3811
Helixi39 – 5416
Turni55 – 573
Helixi63 – 8624
Helixi93 – 10614
Helixi111 – 12111
Helixi125 – 14824
Helixi156 – 1627
Beta strandi174 – 1829
Helixi189 – 20719
Helixi212 – 2198
Helixi225 – 2273
Beta strandi230 – 2345
Helixi236 – 2383
Helixi241 – 2444
Helixi246 – 2483
Beta strandi255 – 2617
Beta strandi264 – 27310
Beta strandi282 – 29211
Beta strandi296 – 2983
Helixi300 – 31516
Helixi321 – 3288
Turni332 – 3343
Helixi335 – 3373
Beta strandi340 – 3445
Helixi346 – 3483
Helixi351 – 3588
Beta strandi375 – 38612
Helixi396 – 42025
Beta strandi423 – 4253

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0ABZ6.
SMRiP0ABZ6. Positions 25-428.

Miscellaneous databases

EvolutionaryTraceiP0ABZ6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini171 – 272102PpiC 1
Add
BLAST
Domaini282 – 382101PpiC 2
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 2 PpiC domains.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG0760.
HOGENOMiHOG000264337.
KOiK03771.
OMAiLGKMQLS.
OrthoDBiEOG6M9DS4.
PhylomeDBiP0ABZ6.

Family and domain databases

HAMAPiMF_01183. Chaperone_SurA.
InterProiIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR023034. PPIase_SurA.
IPR015391. SurA_N.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view]
PfamiPF00639. Rotamase. 2 hits.
PF09312. SurA_N. 1 hit.
[Graphical view]
SUPFAMiSSF109998. SSF109998. 1 hit.
PROSITEiPS01096. PPIC_PPIASE_1. 2 hits.
PS50198. PPIC_PPIASE_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABZ6-1 [UniParc]FASTAAdd to Basket

« Hide

MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK    50
LNAAQARQQL PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI 100
ANIAKQNNMT LDQMRSRLAY DGLNYNTYRN QIRKEMIISE VRNNEVRRRI 150
TILPQEVESL AQQVGNQNDA STELNLSHIL IPLPENPTSD QVNEAESQAR 200
AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP GIFAQALSTA 250
KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD 300
EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD 350
PAFRDALTRL NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM 400
LMNRKFSEEA ASWMQEQRAS AYVKILSN 428
Length:428
Mass (Da):47,284
Last modified:November 8, 2005 - v1
Checksum:i25F6AD4B903CBD8E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251V → D1 Publication
Sequence conflicti116 – 1161S → T1 Publication
Sequence conflicti213 – 2131G → GFG1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC73164.1.
AP009048 Genomic DNA. Translation: BAB96620.2.
M68521 Genomic DNA. Translation: AAA24304.1.
AB013134 Genomic DNA. Translation: BAA34131.1.
PIRiE64726.
RefSeqiNP_414595.1. NC_000913.3.
YP_488359.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73164; AAC73164; b0053.
BAB96620; BAB96620; BAB96620.
GeneIDi12932020.
944812.
KEGGiecj:Y75_p0053.
eco:b0053.
PATRICi32115205. VBIEscCol129921_0054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC73164.1 .
AP009048 Genomic DNA. Translation: BAB96620.2 .
M68521 Genomic DNA. Translation: AAA24304.1 .
AB013134 Genomic DNA. Translation: BAA34131.1 .
PIRi E64726.
RefSeqi NP_414595.1. NC_000913.3.
YP_488359.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M5Y X-ray 3.00 A/B/C/D 21-428 [» ]
2PV1 X-ray 1.30 A 172-274 [» ]
2PV2 X-ray 1.30 A/B/C/D 172-274 [» ]
2PV3 X-ray 3.39 A/B 21-428 [» ]
ProteinModelPortali P0ABZ6.
SMRi P0ABZ6. Positions 25-428.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-35827N.
IntActi P0ABZ6. 10 interactions.
MINTi MINT-1242178.
STRINGi 511145.b0053.

2D gel databases

SWISS-2DPAGEi P0ABZ6.

Proteomic databases

PaxDbi P0ABZ6.
PRIDEi P0ABZ6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73164 ; AAC73164 ; b0053 .
BAB96620 ; BAB96620 ; BAB96620 .
GeneIDi 12932020.
944812.
KEGGi ecj:Y75_p0053.
eco:b0053.
PATRICi 32115205. VBIEscCol129921_0054.

Organism-specific databases

EchoBASEi EB0978.
EcoGenei EG10985. surA.

Phylogenomic databases

eggNOGi COG0760.
HOGENOMi HOG000264337.
KOi K03771.
OMAi LGKMQLS.
OrthoDBi EOG6M9DS4.
PhylomeDBi P0ABZ6.

Enzyme and pathway databases

BioCyci EcoCyc:EG10985-MONOMER.
ECOL316407:JW0052-MONOMER.
MetaCyc:EG10985-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ABZ6.
PROi P0ABZ6.

Gene expression databases

Genevestigatori P0ABZ6.

Family and domain databases

HAMAPi MF_01183. Chaperone_SurA.
InterProi IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR023034. PPIase_SurA.
IPR015391. SurA_N.
IPR027304. Trigger_fact/SurA_dom.
[Graphical view ]
Pfami PF00639. Rotamase. 2 hits.
PF09312. SurA_N. 1 hit.
[Graphical view ]
SUPFAMi SSF109998. SSF109998. 1 hit.
PROSITEi PS01096. PPIC_PPIASE_1. 2 hits.
PS50198. PPIC_PPIASE_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiSURA_ECOLI
AccessioniPrimary (citable) accession number: P0ABZ6
Secondary accession number(s): P21202
, P75630, Q8KIP6, Q8KMY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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