A0AAX0HVS3 · A0AAX0HVS3_XANCG

Function

function

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Chaperone SurA
  • Alternative names
    • Peptidyl-prolyl cis-trans isomerase SurA
      (PPIase SurA
      ) (EC:5.2.1.8
      ) . EC:5.2.1.8 (UniProtKB | ENZYME | Rhea)
    • Rotamase SurA

Gene names

    • Name
      surA
    • ORF names
      BIY41_04590

Organism names

Accessions

  • Primary accession
    A0AAX0HVS3

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for signal, chain.

Type
IDPosition(s)Description
Signal1-25
ChainPRO_504306147126-463Chaperone SurA

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain174-276PpiC
Domain289-388PpiC
Region431-463Disordered
Compositional bias451-463Pro residues

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 to function as a chaperone. The N-terminal region and the C-terminal tail are also required for porin recognition.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    463
  • Mass (Da)
    50,100
  • Last updated
    2024-11-27 v1
  • MD5 Checksum
    C66A2176D4752015C54D03D246091BE5
MTKPFSVVLASLLAITSTVSPLASAQQSQPLDRIAAIVDEDVVLQSELDRAVRNVKSQYAGRENQLPPDDVLQRQVLERLVLVKLQVSRADGNGIRVSDEELNRAIASIAQQNGTTVDGLRQKLAADGMGYADFRASVRDEIIVQRLRQSFAQSRISVSEGEVDTALAQQAATGSQYHLAHILIGLPEGANAEQIATGQKKVDGVKALIDKGELDFSAAAVRYSDSPNALEGGDLGWRSLDEIPNAFAQLIRDMQPGQVAGPLRGPSGFQLLKLVEMRDANAGGEKKMVTEYHARHILVRIGDNQSEAQAKAKIDTIRARIVGGADFQATAKESSEDTNSRGQGGDLGWFPADAFGPDFGKQVESLTDGAVSEPFRTQAGWHIVQRVGSRQTDVSAENQRAQVRETIGRRKLEEEYNRYLQELRGEAYVSYRTGDRADDNATAAPAKSPDPAAPSPPPAKPTR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias451-463Pro residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MKCQ01000022
EMBL· GenBank· DDBJ
OEY88595.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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