ID S1P7Z5_ECOLX Unreviewed; 222 AA.
AC S1P7Z5;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Thiol:disulfide interchange protein DsbL {ECO:0000256|HAMAP-Rule:MF_00932};
DE Flags: Precursor;
GN Name=dsbL {ECO:0000256|HAMAP-Rule:MF_00932};
GN ORFNames=A13A_03375 {ECO:0000313|EMBL:EOW94098.1};
OS Escherichia coli KTE182.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=1181728 {ECO:0000313|EMBL:EOW94098.1, ECO:0000313|Proteomes:UP000014179};
RN [1] {ECO:0000313|EMBL:EOW94098.1, ECO:0000313|Proteomes:UP000014179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTE182 {ECO:0000313|EMBL:EOW94098.1,
RC ECO:0000313|Proteomes:UP000014179};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Nielsen K.L., Frimodt-Moller N., Andersen P.S., Walker B.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J.,
RA Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A.,
RA Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Escherichia coli KTE182.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOW94098.1}.
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DR EMBL; ASUG01000048; EOW94098.1; -; Genomic_DNA.
DR RefSeq; WP_000040020.1; NZ_KE136864.1.
DR AlphaFoldDB; S1P7Z5; -.
DR SMR; S1P7Z5; -.
DR PATRIC; fig|1181728.3.peg.3500; -.
DR HOGENOM; CLU_088255_3_1_6; -.
DR Proteomes; UP000014179; Unassembled WGS sequence.
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_5026398168"
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
//
