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Database: UniProt
Entry: B7N0I6_ECO81
LinkDB: B7N0I6_ECO81
Original site: B7N0I6_ECO81 
ID   B7N0I6_ECO81            Unreviewed;       222 AA.
AC   B7N0I6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Thiol:disulfide interchange protein DsbL {ECO:0000256|HAMAP-Rule:MF_00932};
DE   Flags: Precursor;
GN   Name=dsbA {ECO:0000313|EMBL:CAR09854.2};
GN   Synonyms=dsbL {ECO:0000256|HAMAP-Rule:MF_00932};
GN   OrderedLocusNames=ECED1_3705 {ECO:0000313|EMBL:CAR09854.2};
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397 {ECO:0000313|EMBL:CAR09854.2, ECO:0000313|Proteomes:UP000000748};
RN   [1] {ECO:0000313|Proteomes:UP000000748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a {ECO:0000313|Proteomes:UP000000748};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring
CC       its disulfide bond to other proteins. Part of a redox system composed
CC       of DsbI and DsbL that mediates formation of an essential disulfide bond
CC       in AssT. {ECO:0000256|HAMAP-Rule:MF_00932}.
CC   -!- SUBUNIT: Interacts with DsbI. {ECO:0000256|HAMAP-Rule:MF_00932}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC       ECO:0000256|HAMAP-Rule:MF_00932, ECO:0000256|PIRNR:PIRNR001488}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbL subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00932}.
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DR   EMBL; CU928162; CAR09854.2; -; Genomic_DNA.
DR   RefSeq; WP_000040020.1; NC_011745.1.
DR   AlphaFoldDB; B7N0I6; -.
DR   SMR; B7N0I6; -.
DR   KEGG; ecq:ECED1_3705; -.
DR   HOGENOM; CLU_088255_3_1_6; -.
DR   OMA; YEVAKIQ; -.
DR   Proteomes; UP000000748; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd03019; DsbA_DsbA; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   HAMAP; MF_00932; DsbL; 1.
DR   InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR   InterPro; IPR023205; DsbA/DsbL.
DR   InterPro; IPR028588; DsbL.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR   PANTHER; PTHR35891:SF1; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBL; 1.
DR   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00932,
KW   ECO:0000256|PIRNR:PIRNR001488};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_00932};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00932};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_00932}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00932"
FT   CHAIN           28..222
FT                   /note="Thiol:disulfide interchange protein DsbL"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00932"
FT                   /id="PRO_5026404936"
FT   DOMAIN          14..221
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DISULFID        56..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00932,
FT                   ECO:0000256|PIRSR:PIRSR001488-1"
SQ   SEQUENCE   222 AA;  24381 MW;  02DC1FC21369359D CRC64;
     MSKLGISSLF KTILLTAALA VSFTASAFTE GTDYMVLEKP IPNADKTLIK VFSYACPFCY
     KYDKAVTGPV SEKVKDIVAF TPFHLETKGE YGKQASEVFA VLINKDKAAG ISLFDANSQF
     KKAKFAYYAA YHDKKERWSD GKDPAAFIKT GLDAAGMSQA DFEAALKEPA VQETLEKWKA
     SYDVAKIQGV PAYVVNGKYL IYTKSIKSID AMADLIRELA SK
//
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