ID   DSBE_PASMU              Reviewed;         181 AA.
AC   Q9CPM6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE; Synonyms=ccmG; OrderedLocusNames=PM0011;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02095.1; -; Genomic_DNA.
DR   RefSeq; WP_005722249.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPM6; -.
DR   SMR; Q9CPM6; -.
DR   STRING; 747.DR93_2068; -.
DR   EnsemblBacteria; AAK02095; AAK02095; PM0011.
DR   KEGG; pmu:PM0011; -.
DR   PATRIC; fig|272843.6.peg.11; -.
DR   HOGENOM; CLU_042529_19_1_6; -.
DR   OMA; MIGKPFP; -.
DR   Proteomes; UP000000809; Chromosome.
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..181
FT                   /note="Thiol:disulfide interchange protein DsbE"
FT                   /id="PRO_0000201297"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..181
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          38..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        78..81
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   181 AA;  20660 MW;  75B0192FBE4E64FF CRC64;
     MNKKLYFPLI LFLILVFAFA VQLLRNAQGD DPKALESALI GKPVPLRTLQ DLFEEKQYGI
     EIFQQGKPIL LNVWATWCPT CYAEHQYLNK LAQQGVTIIG IDYKDKSAQA IKWLKDLGNP
     YQIVLKDEKG SNGLDLGVYG APETFVIDGQ GIIHYRHAGD LNQKVWDEKI QPIYQKLVER
     K