DSBE_ECOLI
ID DSBE_ECOLI Reviewed; 185 AA.
AC P0AA86; P33926; Q2MAP8;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Thiol:disulfide interchange protein DsbE;
DE AltName: Full=Cytochrome c biogenesis protein CcmG;
GN Name=dsbE; Synonyms=ccmG, yejQ; OrderedLocusNames=b2195, JW2183;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 1-6, AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=11256948; DOI=10.1042/0264-6021:3550051;
RA Reid E., Cole J., Eaves D.J.;
RT "The Escherichia coli CcmG protein fulfils a specific role in cytochrome c
RT assembly.";
RL Biochem. J. 355:51-58(2001).
RN [5]
RP CHARACTERIZATION.
RX PubMed=7635817; DOI=10.1128/jb.177.15.4321-4326.1995;
RA Thoeny-Meyer L., Fischer F., Kunzler P., Ritz D., Hennecke H.;
RT "Escherichia coli genes required for cytochrome c maturation.";
RL J. Bacteriol. 177:4321-4326(1995).
RN [6]
RP CHARACTERIZATION.
RA Missiakas D., Georgopoulos C., Raina S.;
RL Submitted (NOV-1994) to UniProtKB.
RN [7]
RP MUTAGENESIS OF CYS-80 AND CYS-83.
RX PubMed=9537397; DOI=10.1128/jb.180.7.1947-1950.1998;
RA Fabianek R.A., Hennecke H., Thoeny-Meyer L.;
RT "The active-site cysteines of the periplasmic thioredoxin-like protein CcmG
RT of Escherichia coli are important but not essential for cytochrome c
RT maturation in vivo.";
RL J. Bacteriol. 180:1947-1950(1998).
RN [8]
RP CHARACTERIZATION.
RX PubMed=11350062; DOI=10.1006/bbrc.2001.4876;
RA Li Q., Hu H.-Y., Xu G.-J.;
RT "Biochemical characterization of the thioredoxin domain of Escherichia coli
RT DsbE protein reveals a weak reductant.";
RL Biochem. Biophys. Res. Commun. 283:849-853(2001).
RN [9]
RP CHARACTERIZATION.
RC STRAIN=BL21-DE3;
RX PubMed=11843181; DOI=10.1515/bc.2001.203;
RA Li Q., Hu H.-Y., Wang W.-Q., Xu G.-J.;
RT "Structural and redox properties of the leaderless DsbE (CcmG) protein:
RT both active-site cysteines of the reduced form are involved in its function
RT in the Escherichia coli periplasm.";
RL Biol. Chem. 382:1679-1686(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 DsbE is maintained in a reduced state by DsbD.
CC -!- INTERACTION:
CC P0AA86; P36655: dsbD; NbExp=4; IntAct=EBI-9014059, EBI-9014057;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC protein; Periplasmic side.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000305}.
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DR EMBL; U00008; AAA16387.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75255.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76658.1; -; Genomic_DNA.
DR PIR; A64989; A64989.
DR RefSeq; NP_416699.1; NC_000913.3.
DR RefSeq; WP_000824439.1; NZ_STEB01000002.1.
DR PDB; 1Z5Y; X-ray; 1.94 A; E=43-185.
DR PDB; 2B1K; X-ray; 1.90 A; A=19-185.
DR PDB; 2B1L; X-ray; 1.90 A; A/B=58-185.
DR PDB; 2G0F; X-ray; 2.20 A; A=19-185.
DR PDB; 3K8N; X-ray; 2.30 A; A=1-185.
DR PDBsum; 1Z5Y; -.
DR PDBsum; 2B1K; -.
DR PDBsum; 2B1L; -.
DR PDBsum; 2G0F; -.
DR PDBsum; 3K8N; -.
DR AlphaFoldDB; P0AA86; -.
DR BMRB; P0AA86; -.
DR SMR; P0AA86; -.
DR BioGRID; 4263405; 34.
DR DIP; DIP-48446N; -.
DR IntAct; P0AA86; 2.
DR STRING; 511145.b2195; -.
DR jPOST; P0AA86; -.
DR PaxDb; P0AA86; -.
DR PRIDE; P0AA86; -.
DR EnsemblBacteria; AAC75255; AAC75255; b2195.
DR EnsemblBacteria; BAE76658; BAE76658; BAE76658.
DR GeneID; 66673910; -.
DR GeneID; 949073; -.
DR KEGG; ecj:JW2183; -.
DR KEGG; eco:b2195; -.
DR PATRIC; fig|511145.12.peg.2284; -.
DR EchoBASE; EB1984; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_1_6; -.
DR InParanoid; P0AA86; -.
DR OMA; MIGKPFP; -.
DR PhylomeDB; P0AA86; -.
DR BioCyc; EcoCyc:EG12053-MON; -.
DR BioCyc; MetaCyc:EG12053-MON; -.
DR EvolutionaryTrace; P0AA86; -.
DR PRO; PR:P0AA86; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031237; C:intrinsic component of periplasmic side of plasma membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IDA:EcoCyc.
DR GO; GO:0017004; P:cytochrome complex assembly; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Cytochrome c-type biogenesis; Direct protein sequencing; Disulfide bond;
KW Membrane; Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..185
FT /note="Thiol:disulfide interchange protein DsbE"
FT /id="PRO_0000201293"
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:0000305"
FT MUTAGEN 80
FT /note="C->S: Drastic decrease in activity."
FT /evidence="ECO:0000269|PubMed:9537397"
FT MUTAGEN 83
FT /note="C->S: Drastic decrease in activity."
FT /evidence="ECO:0000269|PubMed:9537397"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:3K8N"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2B1K"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1Z5Y"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2B1K"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:2B1K"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:2B1K"
FT HELIX 133..138
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:2B1K"
FT STRAND 153..161
FT /evidence="ECO:0007829|PDB:2B1K"
FT HELIX 165..170
FT /evidence="ECO:0007829|PDB:2B1K"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:2B1K"
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
