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P0ABZ6

- SURA_ECOLI

UniProt

P0ABZ6 - SURA_ECOLI

Protein

Chaperone SurA

Gene

surA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (08 Nov 2005)
      Previous versions | rss
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    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

    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

    GO - Biological processi

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

    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.

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: EcoliWiki

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20203 PublicationsAdd
    BLAST
    Chaini21 – 428408Chaperone SurAPRO_0000025542Add
    BLAST

    Proteomic databases

    PaxDbiP0ABZ6.
    PRIDEiP0ABZ6.

    2D gel databases

    SWISS-2DPAGEP0ABZ6.

    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

    1
    428
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0ABZ6.

    Family & Domainsi

    Domains and Repeats

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

    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

    Experimental Info

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

    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...
    MobiDBi Search...

    Protein-protein interaction databases

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

    2D gel databases

    SWISS-2DPAGE 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

    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: October 1, 2014
    This is version 81 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