DSBE_YERPE
ID DSBE_YERPE Reviewed; 188 AA.
AC Q8ZD52; Q0WDF1;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Thiol:disulfide interchange protein DsbE;
DE AltName: Full=Cytochrome c biogenesis protein CcmG;
GN Name=dsbE; Synonyms=ccmG; OrderedLocusNames=YPO2740, y1573, YP_2424;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL21359.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM85142.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62629.1; -; Genomic_DNA.
DR PIR; AD0334; AD0334.
DR RefSeq; WP_002209699.1; NZ_WUCM01000012.1.
DR RefSeq; YP_002347687.1; NC_003143.1.
DR AlphaFoldDB; Q8ZD52; -.
DR SMR; Q8ZD52; -.
DR STRING; 214092.YPO2740; -.
DR PaxDb; Q8ZD52; -.
DR DNASU; 1146520; -.
DR EnsemblBacteria; AAM85142; AAM85142; y1573.
DR EnsemblBacteria; AAS62629; AAS62629; YP_2424.
DR GeneID; 66844936; -.
DR KEGG; ype:YPO2740; -.
DR KEGG; ypk:y1573; -.
DR KEGG; ypm:YP_2424; -.
DR PATRIC; fig|214092.21.peg.3183; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_1_6; -.
DR OMA; MIGKPFP; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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..188
FT /note="Thiol:disulfide interchange protein DsbE"
FT /id="PRO_0000201306"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..188
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..186
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 85..88
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 145
FT /note="V -> G (in Ref. 3; AAS62629)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 188 AA; 21072 MW; AEA1967477034A56 CRC64;
MKPQSSFNKL MFIPLVLFLL LVVAFLIQLT RNANGEDPTM LESALIGKPV PAFKLESLEQ
PGKTFDQAVL RDGKPILLNV WATWCPTCRA EHEYLNKLAA QGIRVVGLNY KDDRSKAVQW
LNSLGNPYFL SLYDGDGMLG LDLGVYGAPE TFLIDGQGVI RYRHAGDLND RVWQQEILPL
YKKYQGGA
