ID A0A0A3I8X4_9BACL Unreviewed; 141 AA.
AC A0A0A3I8X4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE SubName: Full=Disulfide bond formation protein DsbB {ECO:0000313|EMBL:KGR79940.1};
GN ORFNames=CD29_02995 {ECO:0000313|EMBL:KGR79940.1};
OS Ureibacillus manganicus DSM 26584.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Caryophanaceae;
OC Ureibacillus.
OX NCBI_TaxID=1384049 {ECO:0000313|EMBL:KGR79940.1, ECO:0000313|Proteomes:UP000030416};
RN [1] {ECO:0000313|EMBL:KGR79940.1, ECO:0000313|Proteomes:UP000030416}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26584 {ECO:0000313|EMBL:KGR79940.1,
RC ECO:0000313|Proteomes:UP000030416};
RA Zhang F., Wang G., Zhang L.;
RT "Draft genome sequence of Lysinibacillus manganicus DSM 26584T.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily.
CC {ECO:0000256|ARBA:ARBA00007602}.
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:KGR79940.1}.
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DR EMBL; JPVN01000003; KGR79940.1; -; Genomic_DNA.
DR RefSeq; WP_036182670.1; NZ_AVDA01000003.1.
DR AlphaFoldDB; A0A0A3I8X4; -.
DR STRING; 1384049.CD29_02995; -.
DR eggNOG; COG1495; Bacteria.
DR OrthoDB; 158402at2; -.
DR Proteomes; UP000030416; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
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 Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000030416};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 39..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 141 AA; 15911 MW; 1A9B6189AF7B28F9 CRC64;
MKKKLENSLL FIWIVSLVAT LGSLYFSEVR GYTPCELCWY QRILMYPIVL MTTIAYIQKN
ARIALTTAVF SVVGGFISLY HYGIQKIDFL SANAPSCGQV PCTGQYINWL GFITIPFLAL
TAFILIAITS FYMLKVLKGE K
//
