Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chaperone SurA

Gene

surA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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.3 Publications

Catalytic activityi

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

GO - Molecular functioni

  • peptide binding Source: EcoCyc
  • peptidyl-prolyl cis-trans isomerase activity Source: EcoCyc
  • unfolded protein binding Source: EcoCyc

GO - Biological processi

  • chaperone cofactor-dependent protein refolding Source: EcoCyc
  • Gram-negative-bacterium-type cell outer membrane assembly Source: EcoliWiki
  • maintenance of stationary phase Source: EcoliWiki
  • protein folding Source: EcoCyc
  • protein stabilization Source: EcoCyc

Keywordsi

Molecular functionChaperone, Isomerase, Rotamase

Enzyme and pathway databases

BioCyciEcoCyc:EG10985-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10985 surA

Subcellular locationi

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

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 203 PublicationsAdd BLAST20
ChainiPRO_000002554221 – 428Chaperone SurAAdd BLAST408

Proteomic databases

EPDiP0ABZ6
PaxDbiP0ABZ6
PRIDEiP0ABZ6

2D gel databases

SWISS-2DPAGEiP0ABZ6

Interactioni

Binary interactionsi

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

GO - Molecular functioni

  • unfolded protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261014, 418 interactors
DIPiDIP-35827N
IntActiP0ABZ6, 10 interactors
STRINGi316385.ECDH10B_0054

Structurei

Secondary structure

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 38Combined sources11
Helixi39 – 54Combined sources16
Turni55 – 57Combined sources3
Helixi63 – 86Combined sources24
Helixi93 – 106Combined sources14
Helixi111 – 121Combined sources11
Helixi125 – 148Combined sources24
Helixi156 – 162Combined sources7
Beta strandi173 – 182Combined sources10
Helixi189 – 207Combined sources19
Helixi212 – 219Combined sources8
Helixi225 – 227Combined sources3
Beta strandi230 – 234Combined sources5
Helixi236 – 238Combined sources3
Helixi241 – 246Combined sources6
Turni247 – 249Combined sources3
Beta strandi255 – 261Combined sources7
Beta strandi264 – 274Combined sources11
Beta strandi282 – 292Combined sources11
Beta strandi296 – 298Combined sources3
Helixi300 – 315Combined sources16
Helixi321 – 328Combined sources8
Turni332 – 334Combined sources3
Helixi335 – 337Combined sources3
Beta strandi340 – 344Combined sources5
Helixi346 – 348Combined sources3
Helixi351 – 358Combined sources8
Beta strandi375 – 386Combined sources12
Helixi396 – 420Combined sources25
Beta strandi423 – 425Combined sources3

3D structure databases

ProteinModelPortaliP0ABZ6
SMRiP0ABZ6
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABZ6

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini171 – 272PpiC 1Add BLAST102
Domaini282 – 382PpiC 2Add BLAST101

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG4105DBD Bacteria
COG0760 LUCA
HOGENOMiHOG000264337
InParanoidiP0ABZ6
KOiK03771
OMAiEMIISRV
PhylomeDBiP0ABZ6

Family and domain databases

HAMAPiMF_01183 Chaperone_SurA, 1 hit
InterProiView protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR023034 PPIase_SurA
IPR015391 SurA_N
IPR027304 Trigger_fact/SurA_dom_sf
PfamiView protein in Pfam
PF00639 Rotamase, 1 hit
PF09312 SurA_N, 1 hit
SUPFAMiSSF109998 SSF109998, 1 hit
PROSITEiView protein in PROSITE
PS01096 PPIC_PPIASE_1, 2 hits
PS50198 PPIC_PPIASE_2, 2 hits

Sequencei

Sequence statusi: Complete.

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

P0ABZ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNWKTLLLG IAMIANTSFA APQVVDKVAA VVNNGVVLES DVDGLMQSVK
60 70 80 90 100
LNAAQARQQL PDDATLRHQI MERLIMDQII LQMGQKMGVK ISDEQLDQAI
110 120 130 140 150
ANIAKQNNMT LDQMRSRLAY DGLNYNTYRN QIRKEMIISE VRNNEVRRRI
160 170 180 190 200
TILPQEVESL AQQVGNQNDA STELNLSHIL IPLPENPTSD QVNEAESQAR
210 220 230 240 250
AIVDQARNGA DFGKLAIAHS ADQQALNGGQ MGWGRIQELP GIFAQALSTA
260 270 280 290 300
KKGDIVGPIR SGVGFHILKV NDLRGESKNI SVTEVHARHI LLKPSPIMTD
310 320 330 340 350
EQARVKLEQI AADIKSGKTT FAAAAKEFSQ DPGSANQGGD LGWATPDIFD
360 370 380 390 400
PAFRDALTRL NKGQMSAPVH SSFGWHLIEL LDTRNVDKTD AAQKDRAYRM
410 420
LMNRKFSEEA ASWMQEQRAS AYVKILSN
Length:428
Mass (Da):47,284
Last modified:November 8, 2005 - v1
Checksum:i25F6AD4B903CBD8E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25V → D (Ref. 1) Curated1
Sequence conflicti116S → T (Ref. 1) Curated1
Sequence conflicti213G → GFG (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000800457.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73164; AAC73164; b0053
BAB96620; BAB96620; BAB96620
GeneIDi944812
KEGGiecj:JW0052
eco:b0053
PATRICifig|1411691.4.peg.2230

Similar proteinsi

Entry informationi

Entry nameiSURA_ECOLI
AccessioniPrimary (citable) accession number: P0ABZ6
Secondary accession number(s): P21202
, P75630, Q8KIP6, Q8KMY0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: March 28, 2018
This is version 109 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health