ID A0A7V7UV91_9BACI Unreviewed; 139 AA.
AC A0A7V7UV91;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=Probable disulfide formation protein {ECO:0000256|HAMAP-Rule:MF_00287};
DE AltName: Full=Disulfide oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00287};
DE AltName: Full=Thiol-disulfide oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00287};
GN Name=bdbC {ECO:0000256|HAMAP-Rule:MF_00287};
GN ORFNames=F7732_12035 {ECO:0000313|EMBL:KAB2332807.1};
OS Bacillus mesophilum.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1071718 {ECO:0000313|EMBL:KAB2332807.1, ECO:0000313|Proteomes:UP000441354};
RN [1] {ECO:0000313|EMBL:KAB2332807.1, ECO:0000313|Proteomes:UP000441354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IITR-54 {ECO:0000313|EMBL:KAB2332807.1,
RC ECO:0000313|Proteomes:UP000441354};
RX PubMed=24807729;
RA Manickam N., Singh N.K., Bajaj A., Kumar R.M., Kaur G., Kaur N., Bala M.,
RA Kumar A., Mayilraj S.;
RT "Bacillus mesophilum sp. nov., strain IITR-54T, a novel 4-chlorobiphenyl
RT dechlorinating bacterium.";
RL Arch. Microbiol. 196:517-523(2014).
CC -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC {ECO:0000256|HAMAP-Rule:MF_00287}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00287};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00287}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily.
CC {ECO:0000256|ARBA:ARBA00007602, ECO:0000256|HAMAP-Rule:MF_00287}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAB2332807.1}.
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DR EMBL; WBOT01000003; KAB2332807.1; -; Genomic_DNA.
DR RefSeq; WP_151574140.1; NZ_WBOT01000003.1.
DR AlphaFoldDB; A0A7V7UV91; -.
DR OrthoDB; 158402at2; -.
DR Proteomes; UP000441354; Unassembled WGS sequence.
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; DsbB-like; 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 NCBIfam; NF002849; PRK03113.1; 1.
DR PANTHER; PTHR43469; DISULFIDE FORMATION PROTEIN-RELATED; 1.
DR PANTHER; PTHR43469:SF1; SPBETA PROPHAGE-DERIVED DISULFIDE BOND FORMATION PROTEIN B; 1.
DR Pfam; PF02600; DsbB; 1.
DR PIRSF; PIRSF036659; BdbC; 1.
DR SUPFAM; SSF158442; DsbB-like; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00287};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00287};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW Rule:MF_00287};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_00287};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00287};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00287};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW Rule:MF_00287}; Reference proteome {ECO:0000313|Proteomes:UP000441354};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00287};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00287};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00287}.
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DISULFID 37..40
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00287"
FT DISULFID 98..104
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00287"
SQ SEQUENCE 139 AA; 16002 MW; A0FAB048819DFA34 CRC64;
MEAQKKSQLF LYLAWVISMI AALGSLYFSE IRGFVPCELC WYQRIFMYPL VFVLGIGAFY
QDHTVKRIAL PMAVIGWCIS IYHYLLQMVP GFAEIKPCAN GVPCNAKYID WFGFVTIPFL
ALTAFTLIIV LLLMMRIKR
//
