MULTISPECIES: thiol:disulfide interchange protein DsbA/DsbL

LOCUS       WP_002540835             200 aa            linear   BCT 29-MAR-2023
            [Grimontia].
ACCESSION   WP_002540835
VERSION     WP_002540835.1
KEYWORDS    RefSeq.
SOURCE      Grimontia
  ORGANISM  Grimontia
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae.
REFERENCE   1  (residues 1 to 200)
  AUTHORS   Qi,Y. and Grishin,N.V.
  TITLE     Structural classification of thioredoxin-like fold proteins
  JOURNAL   Proteins 58 (2), 376-388 (2005)
   PUBMED   15558583
REFERENCE   2  (residues 1 to 200)
  AUTHORS   Kadokura,H., Katzen,F. and Beckwith,J.
  TITLE     Protein disulfide bond formation in prokaryotes
  JOURNAL   Annu Rev Biochem 72, 111-135 (2003)
   PUBMED   12524212
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10122479
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..200
                     /organism="Grimontia"
                     /db_xref="taxon:246861"
     Protein         1..200
                     /product="thiol:disulfide interchange protein DsbA/DsbL"
                     /GO_function="GO:0015035 - protein-disulfide reductase
                     activity [Evidence IEA]"
                     /calculated_mol_wt=22262
     Region          25..197
                     /region_name="DsbA_DsbA"
                     /note="DsbA family, DsbA subfamily; DsbA is a monomeric
                     thiol disulfide oxidoreductase protein containing a redox
                     active CXXC motif imbedded in a TRX fold. It is involved
                     in the oxidative protein folding pathway in prokaryotes,
                     and is the strongest thiol...; cd03019"
                     /db_xref="CDD:239317"
     Site            order(50,52..53,169)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239317"
     Site            80..82
                     /site_type="other"
                     /note="hinge region"
                     /db_xref="CDD:239317"
     Site            order(88..96,101..120,124..132,138..147)
                     /site_type="other"
                     /note="alpha helical domain"
                     /db_xref="CDD:239317"
ORIGIN      
        1 mlkkmlavaa aamlafsaqa arfnagedyq vldlpksdtp svveffsfyc phcfkseplm
       61 qelkknipdn anftknhvsf mggnmgkals kayatavmld vedkmvpvif nrihlmqkpp
      121 rneeelrqmf idegvdaekf dgtfnsfaan gmanrfdkaf qdsglrgvpa livngkyhvt
      181 pktvktkedy falvnflltq