DSBI_CAMJJ
ID DSBI_CAMJJ Reviewed; 269 AA.
AC A1VZK8; Q46097; Q9PP58;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Putative protein-disulfide oxidoreductase DsbI;
GN Name=dsbI; OrderedLocusNames=CJJ81176_0881;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8655516; DOI=10.1128/jb.178.11.3335-3338.1996;
RA Yao R., Guerry P.;
RT "Molecular cloning and site-specific mutagenesis of a gene involved in
RT arylsulfatase production in Campylobacter jejuni.";
RL J. Bacteriol. 178:3335-3338(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some proteins. Part
CC of a redox system composed of DsbI and DsbL that mediates formation of
CC an essential disulfide bond in AssT (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DsbL. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DsbB family. DsbI subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally given the gene name dsbB; however this seems to
CC belong to a different DsbB subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ72274.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U38280; AAB18371.1; -; Genomic_DNA.
DR EMBL; CP000538; EAQ72274.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002869425.1; NC_008787.1.
DR AlphaFoldDB; A1VZK8; -.
DR STRING; 354242.CJJ81176_0881; -.
DR PRIDE; A1VZK8; -.
DR EnsemblBacteria; EAQ72274; EAQ72274; CJJ81176_0881.
DR KEGG; cjj:CJJ81176_0881; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_090583_0_0_7; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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; -; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR023380; DsbB-like_sf.
DR Pfam; PF02600; DsbB; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Disulfide bond; Electron transport;
KW Membrane; Oxidoreductase; Redox-active center; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..269
FT /note="Putative protein-disulfide oxidoreductase DsbI"
FT /id="PRO_0000281900"
FT TRANSMEM 25..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 52..55
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 122..148
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 269 AA; 30798 MW; 2DCD3270E1FC1BE4 CRC64;
MSCIKMKDNC RNFSLSKWQD TRKPWLILII VTIGLTCIAH FLFQEYLFME PCEQCVYIRF
DMLVMAIGGM IALINPTNNI IKIFSYSLAF YGIWLGLEHC LTLNHIHEVV HSENPFAGVD
GCREIPIYPF NLPLHEWAPS WFLPIGECGM DTPVVPENAY NHLNAFQKFF IGTPPDFENG
LYSNGWYLIP SLKFINMAIC CLIAFLCCFI VLFAMFIAYV LDKNKPNAKI FALAIVILVL
VLKFIGEPKN PNQNIASLNH LNQVVLRYS
