ID A0A1H3PPI4_9BACI Unreviewed; 144 AA.
AC A0A1H3PPI4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 17.
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=SAMN05421736_105148 {ECO:0000313|EMBL:SDZ03104.1};
OS Evansella caseinilytica.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Evansella.
OX NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDZ03104.1, ECO:0000313|Proteomes:UP000198935};
RN [1] {ECO:0000313|Proteomes:UP000198935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00287}.
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DR EMBL; FNPI01000005; SDZ03104.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3PPI4; -.
DR STRING; 1503961.SAMN05421736_105148; -.
DR OrthoDB; 158402at2; -.
DR Proteomes; UP000198935; 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:UP000198935};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DISULFID 40..43
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00287"
SQ SEQUENCE 144 AA; 16296 MW; AFAF1E74CC948732 CRC64;
MEETSKQKKI EYAMFAAWGI ALIATLGSLY FSEVKLFMPC SLCWVQRIFM YPLAITLAIA
SVKKDAGQAY YTLPLSLIGL GFSSYHYMLE KIPALSTQAE ACGIIPCNYE YINWFGFITI
PFLALVSFFF ISLMMVYVIK ASKE
//
