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Database: UniProt
Entry: A0A926NGB4_9BACL
LinkDB: A0A926NGB4_9BACL
Original site: A0A926NGB4_9BACL 
ID   A0A926NGB4_9BACL        Unreviewed;       148 AA.
AC   A0A926NGB4;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   18-JUN-2025, entry version 8.
DE   SubName: Full=Disulfide bond formation protein B {ECO:0000313|EMBL:MBD1372813.1};
GN   ORFNames=IC620_10645 {ECO:0000313|EMBL:MBD1372813.1};
OS   Polycladospora coralii.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC   Thermoactinomycetaceae; Polycladospora.
OX   NCBI_TaxID=2771432 {ECO:0000313|EMBL:MBD1372813.1, ECO:0000313|Proteomes:UP000661691};
RN   [1] {ECO:0000313|EMBL:MBD1372813.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IB182357 {ECO:0000313|EMBL:MBD1372813.1};
RA   Huang H., Mo K., Hu Y.;
RT   "A novel bacterium of genus Hazenella, isolated from South China Sea.";
RL   Submitted (SEP-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:MBD1372813.1}.
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DR   EMBL; JACXAH010000014; MBD1372813.1; -; Genomic_DNA.
DR   RefSeq; WP_191138673.1; NZ_JACXAG020000001.1.
DR   Proteomes; UP000661691; 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:UP000661691};
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..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   148 AA;  16465 MW;  A6213332EFE7468D CRC64;
     MSYTADKAQM SSWLLYAAWL IALIAMGGSL YFSEVNGFTP CELCWYQRIL MYPLVLILGV
     AAYRRDLQIT GYVLALSLIG TGLSFYHYLV QKVPAIAQTS SCTVGVPCSG VYINWLGFIT
     IPFLALTAFV LISILMWMIR VQIKNISG
//
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