MULTISPECIES: thiol:disulfide interchange protein DsbA

LOCUS       WP_003096976             211 aa            linear   BCT 20-NOV-2023
            [Pseudomonas].
ACCESSION   WP_003096976
VERSION     WP_003096976.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 211)
  AUTHORS   Shouldice,S.R., Heras,B., Jarrott,R., Sharma,P., Scanlon,M.J. and
            Martin,J.L.
  TITLE     Characterization of the DsbA oxidative folding catalyst from
            Pseudomonas aeruginosa reveals a highly oxidizing protein that
            binds small molecules
  JOURNAL   Antioxid Redox Signal 12 (8), 921-931 (2010)
   PUBMED   19788398
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  :: BlastRule
            Evidence Accession :: NBR013038
            Evidence Source    :: NCBI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..211
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     gene            1..211
                     /gene="dsbA"
     Protein         1..211
                     /product="thiol:disulfide interchange protein DsbA"
                     /calculated_mol_wt=23244
     Region          27..207
                     /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(56,58..59,173)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239317"
     Site            86..88
                     /site_type="other"
                     /note="hinge region"
                     /db_xref="CDD:239317"
     Site            order(93..100,105..124,128..136,142..151)
                     /site_type="other"
                     /note="alpha helical domain"
                     /db_xref="CDD:239317"
ORIGIN      
        1 mrnliltaml amaslfgmaa qaddytagke yvelsspvpv sqpgkievve lfwygcphcy
       61 afeptivpws eklpadvhfv rlpalfggiw nvhgqmfltl esmgvehdvh navfeaihke
      121 hkklatpeem adflagkgvd kekflstyns faikgqmeka kklamayqvt gvptmvvngk
      181 yrfdigsagg peetlklady liekeraaak k