ID   DSBE_SALTY              Reviewed;         185 AA.
AC   Q8XFK6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE1; Synonyms=ccmG1; OrderedLocusNames=STM2248;
GN   and
GN   Name=dsbE2; Synonyms=ccmG2; OrderedLocusNames=STM3813;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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; AE006468; AAL22672.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21150.1; -; Genomic_DNA.
DR   RefSeq; NP_461191.1; NC_003197.2.
DR   RefSeq; NP_462713.1; NC_003197.2.
DR   RefSeq; WP_000828296.1; NC_003197.2.
DR   AlphaFoldDB; Q8XFK6; -.
DR   SMR; Q8XFK6; -.
DR   STRING; 99287.STM2248; -.
DR   PaxDb; Q8XFK6; -.
DR   EnsemblBacteria; AAL21150; AAL21150; STM2248.
DR   EnsemblBacteria; AAL22672; AAL22672; STM3813.
DR   GeneID; 1253770; -.
DR   GeneID; 1255340; -.
DR   KEGG; stm:STM2248; -.
DR   KEGG; stm:STM3813; -.
DR   PATRIC; fig|99287.12.peg.2382; -.
DR   HOGENOM; CLU_042529_19_1_6; -.
DR   OMA; MIGKPFP; -.
DR   PhylomeDB; Q8XFK6; -.
DR   BioCyc; SENT99287:STM3813-MON; -.
DR   Proteomes; UP000001014; 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..185
FT                   /note="Thiol:disulfide interchange protein DsbE"
FT                   /id="PRO_0000201301"
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;  20679 MW;  9B731AA457929C68 CRC64;
     MKRNVLLLPL LIFLLIAAAL LWQLARNAQG DDPTNLESAL TGKPVPAFRL ESLETPGQYY
     QAEVLTQGKP VLLNVWATWC PTCRAEHQYL NQLSAQGIRV VGLNYKDDRA KAVAWLKELG
     NPYALSLSDS DGMLGLDLGV YGAPETFLID GRGIIRYRHA GDLNARVWES ELKPLWDRYS
     REAAQ