ID   DSBE_VIBCH              Reviewed;         184 AA.
AC   Q9KQE9;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE; Synonyms=ccmG; OrderedLocusNames=VC_2051;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Involved in disulfide bond formation. Catalyzes a late,
CC       reductive step in the assembly of periplasmic c-type cytochromes,
CC       probably the reduction of disulfide bonds of the apocytochrome c to
CC       allow covalent linkage with the heme. Possible subunit of a heme lyase
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE003852; AAF95197.1; -; Genomic_DNA.
DR   PIR; E82124; E82124.
DR   RefSeq; NP_231683.1; NC_002505.1.
DR   RefSeq; WP_001035064.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KQE9; -.
DR   SMR; Q9KQE9; -.
DR   STRING; 243277.VC_2051; -.
DR   DNASU; 2613431; -.
DR   EnsemblBacteria; AAF95197; AAF95197; VC_2051.
DR   KEGG; vch:VC_2051; -.
DR   PATRIC; fig|243277.26.peg.1960; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_19_1_6; -.
DR   OMA; MIGKPFP; -.
DR   BioCyc; VCHO:VC2051-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR   CDD; cd03010; TlpA_like_DsbE; 1.
DR   InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00385; dsbE; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Cytochrome c-type biogenesis;
KW   Disulfide bond; Membrane; Redox-active center; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..184
FT                   /note="Thiol:disulfide interchange protein DsbE"
FT                   /id="PRO_0000201303"
FT   TOPO_DOM        1..4
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        26..184
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          39..176
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        79..82
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   184 AA;  20651 MW;  97DAA0CB79D560AD CRC64;
     MNKKILFIPL VAFLLLAGVF ATQLMKNSAG DDPTKLESVL VGKTVPEFRL EDLAEPGKLY
     DQSIFKGEPL LLNVWATWCP TCYAEHQYLN ELAKQGVKII GLNYKDQRDK ATQWLNDLGN
     PYLISLFDGN GMLGLDLGVY GAPETFLIDA NGVIRYRHVG DVNSRNWQET LAPLYEKMLA
     EAKQ