ID   DSBE_ALLVD              Reviewed;         181 AA.
AC   Q46476; D3RVT8;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Thiol:disulfide interchange protein DsbE;
DE   AltName: Full=Cytochrome c biogenesis protein CcmG;
GN   Name=dsbE; Synonyms=ccmG; OrderedLocusNames=Alvin_2180;
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Chen Y.L., Knaff D.B.;
RT   "Characterization of the ccmF and ccmG genes involved in c-type cytochrome
RT   biogenesis in Chromatium vinosum.";
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB04631.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L78437; AAB04631.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP001896; ADC63101.1; -; Genomic_DNA.
DR   RefSeq; WP_012971373.1; NC_013851.1.
DR   AlphaFoldDB; Q46476; -.
DR   SMR; Q46476; -.
DR   STRING; 572477.Alvin_2180; -.
DR   EnsemblBacteria; ADC63101; ADC63101; Alvin_2180.
DR   KEGG; alv:Alvin_2180; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_042529_19_1_6; -.
DR   OMA; MIGKPFP; -.
DR   OrthoDB; 1617952at2; -.
DR   Proteomes; UP000001441; 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_0000201292"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..181
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          36..178
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   DISULFID        76..79
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT   CONFLICT        14..19
FT                   /note="IFLALA -> SFWPW (in Ref. 1; AAB04631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        112
FT                   /note="M -> L (in Ref. 1; AAB04631)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   181 AA;  20244 MW;  25231D84AD96E3DF CRC64;
     MNTSAKRALI PLGIFLALAA LLFYGLQLDP RKIPSPLVDK PAPEFSLPDL KDPNQTLTRD
     ILIGQVSLVN VWASWCPSCR QEHAELMRIA REHGVRVIGF NWKDTRPEAL AMLQRYGDPY
     TVSLYDPDNK AGIDWGVYGA PETFIVDAEG IIRHKRVGPI DAQVWAEEIQ PIVARYQGGK
     P