ID   DSBE_TATCI              Reviewed;         185 AA.
AC   Q9Z645;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE; Synonyms=ccmG;
OS   Tatumella citrea (Pantoea citrea).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Tatumella.
OX   NCBI_TaxID=53336;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1056R;
RX   PubMed=10735866; DOI=10.1128/jb.182.8.2230-2237.2000;
RA   Pujol C.J., Kado C.I.;
RT   "Genetic and biochemical characterization of the pathway in Pantoea citrea
RT   leading to pink disease of pineapple.";
RL   J. Bacteriol. 182:2230-2237(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; AF103874; AAD19543.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Z645; -.
DR   SMR; Q9Z645; -.
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; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..185
FT                   /note="Thiol:disulfide interchange protein DsbE"
FT                   /id="PRO_0000201296"
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..185
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          39..177
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        80..83
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ   SEQUENCE   185 AA;  20727 MW;  7E37857154B2E001 CRC64;
     MNKKILFIPL VLFLLLAAAL LWQFNRNADG DDPTLLESAL VGKPVPVFKL ESLQNPGQLY
     SQKALINGKP LLLNVWATWC PTCRAEHEYL NTLAEKGVRV VGLNYKDNRV KAINWLNTLG
     NPYALSLYDG DGMLGLDLGV YGAPETFLID GKGIIRYRHA GDLNAEVWKD EVQPLWNKYS
     KLAED