BDBC_COXB1
ID BDBC_COXB1 Reviewed; 147 AA.
AC B6J6V9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Probable disulfide formation protein {ECO:0000255|HAMAP-Rule:MF_00287};
DE AltName: Full=Disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00287};
DE AltName: Full=Thiol-disulfide oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00287};
GN OrderedLocusNames=CbuK_0753;
OS Coxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434924;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuK_Q154;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
CC -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00287}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00287}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00287}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00287}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001020; ACJ20008.1; -; Genomic_DNA.
DR RefSeq; WP_012570717.1; NC_011528.1.
DR AlphaFoldDB; B6J6V9; -.
DR KEGG; cbc:CbuK_0753; -.
DR HOGENOM; CLU_128688_0_0_6; -.
DR OMA; INWFGFI; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00287; BdbC; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR012187; Disulphide_bond_form_BdbC.
DR InterPro; IPR023380; DsbB-like_sf.
DR PANTHER; PTHR43469; PTHR43469; 1.
DR Pfam; PF02600; DsbB; 1.
DR PIRSF; PIRSF036659; BdbC; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Chaperone; Disulfide bond;
KW Electron transport; Membrane; Oxidoreductase; Redox-active center;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..147
FT /note="Probable disulfide formation protein"
FT /id="PRO_1000114969"
FT TRANSMEM 9..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 69..86
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT TRANSMEM 115..138
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 38..41
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
FT DISULFID 99..106
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00287"
SQ SEQUENCE 147 AA; 16866 MW; D19EDC4E43416565 CRC64;
MMVFRLLKNY SLYFAWLTAL IATLGSLYLS LVRHIPVCDL CWYQRVCIYP LTILLGIAAY
RTDRGVVKYA LPLVVLGFLF SIYQYLQQMI PGFAPINLCG STSPHCSEIH WEIFGFITLP
FLGMLATLIM SFFLIMAFYS LDKRLAN
