DSBE_SHIFL
ID DSBE_SHIFL Reviewed; 185 AA.
AC P0AA88; P33926;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Thiol:disulfide interchange protein DsbE;
DE AltName: Full=Cytochrome c biogenesis protein CcmG;
GN Name=dsbE; Synonyms=ccmG; OrderedLocusNames=SF2279, S2409;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43798.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17615.1; -; Genomic_DNA.
DR RefSeq; NP_708091.1; NC_004337.2.
DR RefSeq; WP_000824439.1; NZ_WPGW01000022.1.
DR AlphaFoldDB; P0AA88; -.
DR BMRB; P0AA88; -.
DR SMR; P0AA88; -.
DR STRING; 198214.SF2279; -.
DR EnsemblBacteria; AAN43798; AAN43798; SF2279.
DR EnsemblBacteria; AAP17615; AAP17615; S2409.
DR GeneID; 1027269; -.
DR GeneID; 66673910; -.
DR KEGG; sfl:SF2279; -.
DR KEGG; sfx:S2409; -.
DR PATRIC; fig|198214.7.peg.2730; -.
DR HOGENOM; CLU_042529_19_1_6; -.
DR OMA; MIGKPFP; -.
DR OrthoDB; 1617952at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000201302"
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; 20809 MW; A599F7B77806A6B5 CRC64;
MKRKVLLIPL IIFLAIAAAL LWQLARNAEG DDPTNLESAL IGKPVPKFRL ESLDNPGQFY
QADVLTQGKP VLLNVWATWC PTCRAEHQYL NQLSAQGIRV VGMNYKDDRQ KAISWLKELG
NPYALSLFDG DGMLGLDLGV YGAPETFLID GNGIIRYRHA GDLNPRVWEE EIKPLWEKYS
KEAAQ
