DsbE family thiol:disulfide interchange protein [Grimontia

LOCUS       WP_005506618             184 aa            linear   BCT 28-JUL-2019
            hollisae].
ACCESSION   WP_005506618
VERSION     WP_005506618.1
KEYWORDS    RefSeq.
SOURCE      Grimontia hollisae
  ORGANISM  Grimontia hollisae
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Vibrionales; Vibrionaceae; Grimontia.
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  :: HMM
            Evidence Accession :: TIGR00385.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..184
                     /organism="Grimontia hollisae"
                     /db_xref="taxon:673"
     Protein         1..184
                     /product="DsbE family thiol:disulfide interchange protein"
                     /GO_component="GO:0030288 - outer membrane-bounded
                     periplasmic space [Evidence IEA]"
                     /GO_function="GO:0015036 - disulfide oxidoreductase
                     activity [Evidence IEA]"
                     /GO_process="GO:0017004 - cytochrome complex assembly
                     [Evidence IEA]"
                     /calculated_mol_wt=20343
     Region          1..182
                     /region_name="Protein Disulfide Oxidoreductases and Other
                     Proteins with a Thioredoxin fold"
                     /note="The thioredoxin (TRX)-like superfamily is a large,
                     diverse group of proteins containing a TRX fold. Many
                     members contain a classic TRX domain with a redox active
                     CXXC motif. They function as protein disulfide
                     oxidoreductases (PDOs), altering the redox...; cl00388"
                     /db_xref="CDD:469754"
     Site            order(79,82)
                     /site_type="active"
                     /note="catalytic residues [active]"
                     /db_xref="CDD:239308"
     Site            106..128
                     /site_type="active"
                     /note="central insert [active]"
                     /db_xref="CDD:239308"
ORIGIN      
        1 mkkpllfipf alfmllvavf fvqlgknaeg ddptklesvl vgkpvpafrl edlaeagkly
       61 dqdifhgepl llnvwatwcp tcyaehtyln klaaegvkii glnykddrvk aigwlnslgn
      121 pylvslfdgd gllgldlgvy gapetflida dgiiryrhvg dvnernwndt lrpmyealva
      181 eakg