ID   DSBL_KLEPN              Reviewed;         222 AA.
AC   P0A4L8; P97037;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 59.
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};
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K-36;
RX   PubMed=8887346; DOI=10.1111/j.1348-0421.1996.tb01105.x;
RA   Baek M.C., Kim S.K., Kim D.H., Kim B.K., Choi E.C.;
RT   "Cloning and sequencing of the Klebsiella K-36 astA gene, encoding an
RT   arylsulfate sulfotransferase.";
RL   Microbiol. Immunol. 40:531-537(1996).
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; U32616; AAB49809.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0A4L8; -.
DR   SMR; P0A4L8; -.
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_0000034256"
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;  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