A0A844HY83 · A0A844HY83_9GAMM

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

GO annotations

AspectTerm
Cellular Componentouter membrane-bounded periplasmic space
Molecular Functionpeptide binding
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Molecular Functionunfolded protein binding
Biological ProcessGram-negative-bacterium-type cell outer membrane assembly
Biological Processprotein folding
Biological Processprotein stabilization

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
      FH752_03515

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MES15
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Marinobacteraceae > Marinobacter

Accessions

  • Primary accession
    A0A844HY83

Proteomes

Subcellular Location

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

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_503318798027-446Chaperone SurA

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain177-278PpiC
Domain288-387PpiC

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
    446
  • Mass (Da)
    50,015
  • Last updated
    2021-09-29 v1
  • Checksum
    FC1145AAB7D3B515
MKATLRHGVKALLVLLAVLAPLSVQAERKLLDQVVAIVDEDVILQTELEARISTITSRLSAQGTALPPRQILEERVLDQLITESIQMQMADRAGMRISDNELNETMANIAERNGMSLAQFENQLAAEGVSYNQAREQIRREMLTSRVQQRQVGNRVRVTDREVENYLESLEARGGNNAQYRLAYIFVSVDDPSDEAEVDAAREKAQRLRNEIASGRDFREVAVAESDASNALEGGDMGWRAEGQLPSLVAPVVPELPVGQPSEVLENNSGFHLVMVMDKRGGEQQQLIRQHRVRHILVRPSEATTDSQAETMIRDLYQQLQNGASFSALAKEYSDDPVSGSDGGNLGWVSPGQMVPAFEQAMLNADIGEFQGPFRSQFGWHILQVQERRQKDISGDVRDAEARQAIYRRKFETELQNWLQEIRDEAFIEFKGEYAKDEPAEQEPVS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VENC01000003
EMBL· GenBank· DDBJ
MTI97671.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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