DSBA_SHIFL
ID DSBA_SHIFL Reviewed; 208 AA.
AC P52235;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; OrderedLocusNames=SF3931, S3816;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=YSH6000 / Serotype 2a;
RX PubMed=7761426; DOI=10.1073/pnas.92.11.4927;
RA Watarai M., Tobe T., Yoshikawa M., Sasakawa C.;
RT "Disulfide oxidoreductase activity of Shigella flexneri is required for
RT release of Ipa proteins and invasion of epithelial cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4927-4931(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38253; BAA07407.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN45366.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18832.1; -; Genomic_DNA.
DR RefSeq; NP_709659.1; NC_004337.2.
DR RefSeq; WP_000725335.1; NZ_WPGW01000069.1.
DR PDB; 3DKS; X-ray; 1.90 A; A/B/C/D=20-208.
DR PDBsum; 3DKS; -.
DR AlphaFoldDB; P52235; -.
DR BMRB; P52235; -.
DR SMR; P52235; -.
DR STRING; 198214.SF3931; -.
DR PRIDE; P52235; -.
DR EnsemblBacteria; AAN45366; AAN45366; SF3931.
DR EnsemblBacteria; AAP18832; AAP18832; S3816.
DR GeneID; 1023438; -.
DR KEGG; sfl:SF3931; -.
DR KEGG; sft:NCTC1_04252; -.
DR KEGG; sfx:S3816; -.
DR PATRIC; fig|198214.7.peg.4631; -.
DR HOGENOM; CLU_088255_3_0_6; -.
DR OMA; NAIHKQK; -.
DR OrthoDB; 1805428at2; -.
DR EvolutionaryTrace; P52235; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..208
FT /note="Thiol:disulfide interchange protein DsbA"
FT /id="PRO_0000034267"
FT DOMAIN 20..150
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 68
FT /note="K -> I (in Ref. 1; BAA07407)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> V (in Ref. 1; BAA07407)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="A -> E (in Ref. 1; BAA07407)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="A -> E (in Ref. 1; BAA07407)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..185
FT /note="QGM -> KGL (in Ref. 1; BAA07407)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="E -> K (in Ref. 1; BAA07407)"
FT /evidence="ECO:0000305"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:3DKS"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3DKS"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:3DKS"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3DKS"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:3DKS"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:3DKS"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3DKS"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3DKS"
FT HELIX 190..205
FT /evidence="ECO:0007829|PDB:3DKS"
SQ SEQUENCE 208 AA; 23105 MW; 105A5E876FCAEE55 CRC64;
MKKIWLALAG LVLAFSASAA QYEDGKQYTT LEKPVAGAPQ VLEFFSFFCP HCYQFEEVLH
ISDNVKKKLP EGVKMTKYHV NFMGGDLGKD LTQAWAVAMA LGVEDKVTVP LFEGVQKTQT
IRSASDIRDV FINAGIKGEE YDAAWNSFVV KSLVAQQEKA AADVQLRGVP AMFVNGKYQL
NPQGMDTSNM DVFVQQYADT VKYLSEEK
