DSBA_SALTY
ID DSBA_SALTY Reviewed; 207 AA.
AC P0A2H9; O30848; O69191;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; OrderedLocusNames=STM3997;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=11575497; DOI=10.1139/w01-071;
RA Turcot I., Ponnampalam T.V., Bouwman C.W., Martin N.L.;
RT "Isolation and characterization of a chromosomally encoded disulphide
RT oxidoreductase from Salmonella enterica serovar Typhimurium.";
RL Can. J. Microbiol. 47:711-721(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins such as PhoA or OmpA. Acts by transferring its disulfide bond
CC to other proteins and is reduced in the process. DsbA is reoxidized by
CC DsbB. It is required for pilus biogenesis (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
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DR EMBL; AF019110; AAB81592.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22836.1; -; Genomic_DNA.
DR RefSeq; NP_462877.1; NC_003197.2.
DR RefSeq; WP_000725364.1; NC_003197.2.
DR PDB; 3L9S; X-ray; 1.58 A; A=19-207.
DR PDBsum; 3L9S; -.
DR AlphaFoldDB; P0A2H9; -.
DR SMR; P0A2H9; -.
DR STRING; 99287.STM3997; -.
DR PaxDb; P0A2H9; -.
DR PRIDE; P0A2H9; -.
DR EnsemblBacteria; AAL22836; AAL22836; STM3997.
DR GeneID; 1255523; -.
DR KEGG; stm:STM3997; -.
DR PATRIC; fig|99287.12.peg.4211; -.
DR HOGENOM; CLU_088255_3_0_6; -.
DR OMA; NAIHKQK; -.
DR PhylomeDB; P0A2H9; -.
DR BioCyc; SENT99287:STM3997-MON; -.
DR EvolutionaryTrace; P0A2H9; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR CDD; cd03019; DsbA_DsbA; 1.
DR InterPro; IPR001853; DSBA-like_thioredoxin_dom.
DR InterPro; IPR023205; DsbA/DsbL.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF01323; DSBA; 1.
DR PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Periplasm; Redox-active center;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..207
FT /note="Thiol:disulfide interchange protein DsbA"
FT /id="PRO_0000034266"
FT DOMAIN 20..158
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 49..52
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 139
FT /note="D -> N (in Ref. 1; AAB81592)"
FT /evidence="ECO:0000305"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 123..132
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 147..162
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3L9S"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:3L9S"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3L9S"
FT HELIX 189..205
FT /evidence="ECO:0007829|PDB:3L9S"
SQ SEQUENCE 207 AA; 22911 MW; 8260C50145FD3655 CRC64;
MKKIWLALAG MVLAFSASAA QISDGKQYIT LDKPVAGEPQ VLEFFSFYCP HCYQFEEVLH
VSDNVKKKLP EGTKMTKYHV EFLGPLGKEL TQAWAVAMAL GVEDKVTVPL FEAVQKTQTV
QSAADIRKVF VDAGVKGEDY DAAWNSFVVK SLVAQQEKAA ADLQLQGVPA MFVNGKYQIN
PQGMDTSSMD VFVQQYADTV KYLVDKK
