ID A0A0Q7J414_9BACL Unreviewed; 139 AA.
AC A0A0Q7J414;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE SubName: Full=Disulfide oxidoreductase {ECO:0000313|EMBL:KQX47101.1};
GN ORFNames=ASD40_17715 {ECO:0000313|EMBL:KQX47101.1};
OS Paenibacillus sp. Root444D2.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=1736538 {ECO:0000313|EMBL:KQX47101.1, ECO:0000313|Proteomes:UP000051657};
RN [1] {ECO:0000313|EMBL:KQX47101.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX47101.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX47101.1, ECO:0000313|Proteomes:UP000051657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root444D2 {ECO:0000313|EMBL:KQX47101.1,
RC ECO:0000313|Proteomes:UP000051657};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQX47101.1}.
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DR EMBL; LMEO01000050; KQX47101.1; -; Genomic_DNA.
DR RefSeq; WP_057307027.1; NZ_LMEO01000050.1.
DR AlphaFoldDB; A0A0Q7J414; -.
DR STRING; 1736538.ASD40_17715; -.
DR Proteomes; UP000051657; 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:UP000051657};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 139 AA; 15871 MW; 55224D01314225B9 CRC64;
MSNKWLRDNG MHLSWLLALI ATLGSLYFSE IMNFIPCKLC WYQRILMYPL VVLLGIAAVR
RDYKLTIYVL PLTIWGACIS IYHVLLQSGV FHESATSCGP IPCDVDYLNW LGFITIPMLA
GTAFILITIL QFMTYRATK
//
