ID   A0A7W1XR86_9BACL        Unreviewed;       139 AA.
AC   A0A7W1XR86;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   18-JUN-2025, entry version 9.
DE   SubName: Full=Disulfide bond formation protein B {ECO:0000313|EMBL:MBA4601665.1};
GN   ORFNames=H2C83_04880 {ECO:0000313|EMBL:MBA4601665.1};
OS   Thermoactinomyces mirandus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC   Thermoactinomycetaceae; Thermoactinomyces.
OX   NCBI_TaxID=2756294 {ECO:0000313|EMBL:MBA4601665.1, ECO:0000313|Proteomes:UP000538292};
RN   [1] {ECO:0000313|EMBL:MBA4601665.1, ECO:0000313|Proteomes:UP000538292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMNI-1 {ECO:0000313|EMBL:MBA4601665.1,
RC   ECO:0000313|Proteomes:UP000538292};
RA   Dunlap C.;
RT   "Thermoactinomyces phylogeny.";
RL   Submitted (JUL-2020) 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:MBA4601665.1}.
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; JACEOL010000014; MBA4601665.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7W1XR86; -.
DR   Proteomes; UP000538292; 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:UP000538292};
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..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        40..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        65..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   139 AA;  15968 MW;  B4F1A385638E3A5D CRC64;
     MKSFMKKYSL YFAWLISLVA TSGSLFFSDV LDYTPCTLCW WQRIFMFPLV IVLGIAAYRD
     DRRIVPYVLP LSVLGTGVAF YQYLLQKIPP LTQVSACEAG IPCDKEYINL FGFITFPFLS
     MIAFILIFVC LWVARKTAE
//