DSBE_XYLFT
ID DSBE_XYLFT Reviewed; 197 AA.
AC Q87BH3;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Thiol:disulfide interchange protein DsbE;
DE AltName: Full=Cytochrome c biogenesis protein CcmG;
GN Name=dsbE; Synonyms=ccmG; OrderedLocusNames=PD_1480;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(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; AE009442; AAO29324.1; -; Genomic_DNA.
DR RefSeq; WP_004088487.1; NC_004556.1.
DR AlphaFoldDB; Q87BH3; -.
DR SMR; Q87BH3; -.
DR EnsemblBacteria; AAO29324; AAO29324; PD_1480.
DR GeneID; 58017003; -.
DR KEGG; xft:PD_1480; -.
DR HOGENOM; CLU_042529_19_1_6; -.
DR OMA; ANYIPIT; -.
DR Proteomes; UP000002516; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..197
FT /note="Thiol:disulfide interchange protein DsbE"
FT /id="PRO_0000201305"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..197
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 43..181
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 83..86
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 197 AA; 21694 MW; B5055F95DB0B510B CRC64;
MSDSPRRFPT PLLLTGVMGV LILIALLTFT LMRSWDNASD QSALLGKPAP NFSLPLLHDP
SLQISNTDLA GAPYLLHVWG SWCAACATEQ PVLTHFALSK RVRVIGYNWK DRREDALQWL
EQLGNPYLAV VSDPEGKTAI DWGVTAAPTT FLIDGRGIVR WHHKGALNQQ MIEHKLLPIL
ADIEHSPTAA PALHQAP