DSBL_ECOL6
ID DSBL_ECOL6 Reviewed; 222 AA.
AC P0A4L7; P97037;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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}; OrderedLocusNames=c3786;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 28-222, PARTIAL PROTEIN SEQUENCE
RP OF N-TERMINUS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-56 AND CYS-59, INDUCTION, AND
RP DISULFIDE BOND.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=18565543; DOI=10.1016/j.jmb.2008.05.031;
RA Grimshaw J.P., Stirnimann C.U., Brozzo M.S., Malojcic G., Grutter M.G.,
RA Capitani G., Glockshuber R.;
RT "DsbL and DsbI form a specific dithiol oxidase system for periplasmic
RT arylsulfate sulfotransferase in uropathogenic Escherichia coli.";
RL J. Mol. Biol. 380:667-680(2008).
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 ECO:0000269|PubMed:18565543}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -95 mV. {ECO:0000269|PubMed:18565543};
CC -!- SUBUNIT: Interacts with DsbI. {ECO:0000255|HAMAP-Rule:MF_00932,
CC ECO:0000269|PubMed:18565543}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00932,
CC ECO:0000269|PubMed:18565543}.
CC -!- INDUCTION: Expressed from a tri-cistronic operon that encodes AssT,
CC DsbI and DsbL. {ECO:0000269|PubMed:18565543}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbL subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00932}.
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DR EMBL; AE014075; AAN82230.1; -; Genomic_DNA.
DR RefSeq; WP_000040020.1; NC_004431.1.
DR PDB; 3C7M; X-ray; 1.55 A; A/B=28-222.
DR PDBsum; 3C7M; -.
DR AlphaFoldDB; P0A4L7; -.
DR SMR; P0A4L7; -.
DR STRING; 199310.c3786; -.
DR TCDB; 5.A.2.1.2; the disulfide bond oxidoreductase b (dsbb) family.
DR EnsemblBacteria; AAN82230; AAN82230; c3786.
DR KEGG; ecc:c3786; -.
DR eggNOG; COG2761; Bacteria.
DR HOGENOM; CLU_088255_3_1_6; -.
DR OMA; YEVAKIQ; -.
DR BioCyc; ECOL199310:C3786-MON; -.
DR EvolutionaryTrace; P0A4L7; -.
DR Proteomes; UP000001410; 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 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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Periplasm;
KW Redox-active center; Signal.
FT SIGNAL 1..27
FT CHAIN 28..222
FT /note="Thiol:disulfide interchange protein DsbL"
FT /id="PRO_0000034255"
FT DOMAIN 28..221
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000305"
FT DISULFID 56..59
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691,
FT ECO:0000269|PubMed:18565543"
FT MUTAGEN 56
FT /note="C->S: Loss of activity; when associated with S-59."
FT /evidence="ECO:0000269|PubMed:18565543"
FT MUTAGEN 59
FT /note="C->S: Loss of activity; when associated with S-56."
FT /evidence="ECO:0000269|PubMed:18565543"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:3C7M"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:3C7M"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:3C7M"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:3C7M"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:3C7M"
FT TURN 138..142
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 144..155
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 169..177
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:3C7M"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:3C7M"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3C7M"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3C7M"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3C7M"
FT HELIX 209..220
FT /evidence="ECO:0007829|PDB:3C7M"
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
