ID   DSBE_PSEFC              Reviewed;         178 AA.
AC   P52237; Q51754;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE; Synonyms=ccmG, cyt5, tipB;
OS   Pseudomonas fluorescens biotype C.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=335;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 17400 / DSM 50117 / ICPB 2656-18 / NBRC 15833 / NCIMB 10460 /
RC   Stanier C-18;
RX   PubMed=8878040; DOI=10.1046/j.1365-2958.1996.391399.x;
RA   Gaballa A., Koedam N., Cornelis P.;
RT   "A cytochrome c biogenesis gene involved in pyoverdine production in
RT   Pseudomonas fluorescens ATCC 17400.";
RL   Mol. Microbiol. 21:777-785(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=09906;
RX   PubMed=8692990; DOI=10.1073/pnas.93.14.7315;
RA   Yang C.-H., Azad H.R., Cooksey D.A.;
RT   "A chromosomal locus required for copper resistance, competitive fitness,
RT   and cytochrome c biogenesis in Pseudomonas fluorescens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:7315-7320(1996).
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; Z47979; CAA88019.1; -; Genomic_DNA.
DR   EMBL; U44827; AAC44227.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52237; -.
DR   SMR; P52237; -.
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; IPR013766; Thioredoxin_domain.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR00385; dsbE; 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..178
FT                   /note="Thiol:disulfide interchange protein DsbE"
FT                   /id="PRO_0000201299"
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..178
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          34..178
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        73..76
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        8
FT                   /note="V -> L (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        34
FT                   /note="R -> A (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        44
FT                   /note="N -> S (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        49
FT                   /note="H -> Q (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        60
FT                   /note="R -> I (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="I -> V (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="Y -> F (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163..164
FT                   /note="DE -> EQ (in Ref. 1; CAA88019)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  20043 MW;  83BF444DCD8BF679 CRC64;
     MKRWLMVVPL ALFLLVAVFL YRGLYLDPAE LPSRMIGKPF PAFNLPTVHG DKTLTQADLR
     GKPALVNVWA TWCISCRVEH PVLNKLAEKG VVIYGINYKD DNAAALKWLA EFHNPYQLDI
     RDEDGNLGLN LGVYGAPETF FIDAKGVIRD KYVGVIDEVV WRDELAAKYQ ALVDEAKP