ID   DSBL_LELAM              Reviewed;         222 AA.
AC   Q9XDP1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Thiol:disulfide interchange protein DsbL {ECO:0000255|HAMAP-Rule:MF_00932};
DE   Flags: Precursor;
GN   Name=dsbL {ECO:0000255|HAMAP-Rule:MF_00932}; Synonyms=dsbA;
OS   Lelliottia amnigena (Enterobacter amnigenus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Lelliottia.
OX   NCBI_TaxID=61646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AR-37;
RX   PubMed=10600454; DOI=10.1006/prep.1999.1129;
RA   Kwon A.-R., Oh T.-G., Kim D.-H., Choi E.-C.;
RT   "Molecular cloning of the arylsulfate sulfotransferase gene and
RT   characterization of its product from Enterobacter amnigenus AR-37.";
RL   Protein Expr. Purif. 17:366-372(1999).
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:0000255|HAMAP-Rule:MF_00932}.
CC   -!- SUBUNIT: Interacts with DsbI. {ECO:0000255|HAMAP-Rule:MF_00932}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00932}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbL subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00932}.
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DR   EMBL; AF012826; AAD41461.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XDP1; -.
DR   SMR; Q9XDP1; -.
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   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   Pfam; PF01323; DSBA; 1.
DR   PIRSF; PIRSF001488; Tdi_protein; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Periplasm; Redox-active center; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00932"
FT   CHAIN           28..222
FT                   /note="Thiol:disulfide interchange protein DsbL"
FT                   /id="PRO_0000034257"
FT   DOMAIN          28..221
FT                   /note="Thioredoxin"
FT   DISULFID        56..59
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00932"
SQ   SEQUENCE   222 AA;  24543 MW;  AF2F5B00A8952199 CRC64;
     MSAKWINSIF KSVVLTAALA LPFTASAFTE GTDYMVLEKP IPDADKTLIK VFSYACPFCY
     KYDKAVTGPV ADKVADLVTF VPFHLETKGE YGKQASELFA VTMAKDKAAG VSLFDEKSQF
     KKAKFAWYAA YHDKKERWSD GKDPAAFLKT GLDAAGMSQA EFEAALKEPA VQQTLQKWKA
     AYEVAKIQGV PAYVVNGKYL IYTKNIKSID SMAQLVRELA TK