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Q8KA01

- SURA_BUCAP

UniProt

Q8KA01 - SURA_BUCAP

Protein

Chaperone SurA

Gene

surA

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
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    Functioni

    Chaperone involved in the correct folding and assembly of outer membrane proteins. 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 By similarity.By similarity

    Catalytic activityi

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

    GO - Molecular functioni

    1. peptide binding Source: InterPro
    2. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. biofilm formation Source: InterPro
    2. chaperone mediated protein folding requiring cofactor Source: InterPro
    3. Gram-negative-bacterium-type cell outer membrane assembly Source: InterPro
    4. maintenance of stationary phase Source: InterPro
    5. protein stabilization Source: InterPro

    Keywords - Molecular functioni

    Chaperone, Isomerase, Rotamase

    Enzyme and pathway databases

    BioCyciBAPH198804:GHMG-143-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
    Gene namesi
    Name:surA
    Ordered Locus Names:BUsg_133
    OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
    Taxonomic identifieri198804 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
    ProteomesiUP000000416: Chromosome

    Subcellular locationi

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

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 432411Chaperone SurAPRO_0000025541Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi198804.BUsg133.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8KA01.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini175 – 276102PpiC 1Add
    BLAST
    Domaini286 – 386101PpiC 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 to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition By similarity.By similarity

    Sequence similaritiesi

    Contains 2 PpiC domains.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG0760.
    KOiK03771.
    OMAiLGKMQLS.
    OrthoDBiEOG6M9DS4.

    Family and domain databases

    HAMAPiMF_01183. Chaperone_SurA.
    InterProiIPR000297. PPIase_PpiC.
    IPR023034. PPIase_SurA.
    IPR015391. SurA_N.
    IPR027304. Trigger_fact/SurA_dom.
    [Graphical view]
    PfamiPF00639. Rotamase. 1 hit.
    PF09312. SurA_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF109998. SSF109998. 1 hit.
    PROSITEiPS50198. PPIC_PPIASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8KA01-1 [UniParc]FASTAAdd to Basket

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    MKVYFFLILY VFLSFFSITY SKELEIDKII AIVNNQIILN SDVNQVLFSL    50
    KEEDQRVKIP LKINFLRNKI IKKLITETLI LEEAKKFNIV VTDDQVNNVL 100
    SKYALKKNIT IEELKRNILM NNTNTSFSYN DYFNKIKNSL KVKIIQDYVL 150
    HNRVHISEKE VDLFLNKLIN TQNELKKIDI NCIFLPFIKE KNKIFIKNTK 200
    ILADHFAKKI KKDASFNYYY EYFKKNNNIF LSKEIRSKSL KYLKKIFLNK 250
    LKIIKKNQIL GPILGLKGFY ILKINKIENE NKENLTTEFH IQHCLIRPSV 300
    ILDDKQAKNS IYYIYNNIKN KKYSFDYAVQ KLSHDVYSSH KKGDLGWIST 350
    DFFSNDFRNF LTDLRKNEIS KPIKSNFGWH IIKLLDIRQV DKSNRIDKNL 400
    VYRFLLEKKI KKERYNWIRQ LKKSSYIKIF KN 432
    Length:432
    Mass (Da):51,748
    Last modified:October 1, 2002 - v1
    Checksum:i698284DB452257ED
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67701.1.
    RefSeqiNP_660490.1. NC_004061.1.
    WP_011053668.1. NC_004061.1.

    Genome annotation databases

    EnsemblBacteriaiAAM67701; AAM67701; BUsg_133.
    GeneIDi1005950.
    KEGGibas:BUsg133.
    PATRICi21247047. VBIBucAph100086_0137.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE013218 Genomic DNA. Translation: AAM67701.1 .
    RefSeqi NP_660490.1. NC_004061.1.
    WP_011053668.1. NC_004061.1.

    3D structure databases

    ProteinModelPortali Q8KA01.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 198804.BUsg133.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAM67701 ; AAM67701 ; BUsg_133 .
    GeneIDi 1005950.
    KEGGi bas:BUsg133.
    PATRICi 21247047. VBIBucAph100086_0137.

    Phylogenomic databases

    eggNOGi COG0760.
    KOi K03771.
    OMAi LGKMQLS.
    OrthoDBi EOG6M9DS4.

    Enzyme and pathway databases

    BioCyci BAPH198804:GHMG-143-MONOMER.

    Family and domain databases

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

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sg.

    Entry informationi

    Entry nameiSURA_BUCAP
    AccessioniPrimary (citable) accession number: Q8KA01
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 67 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

    Complete proteome

    Documents

    1. Buchnera aphidicola (subsp. Schizaphis graminum)
      Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3