ID DSBA_PSEAB Reviewed; 211 AA. AC Q02DM0; P95460; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 02-SEP-2026, entry version 92. DE RecName: Full=Thiol:disulfide interchange protein DsbA; DE Flags: Precursor; GN Name=dsbA; OrderedLocusNames=PA14_72450; OS Pseudomonas aeruginosa (strain UCBPP-PA14). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208963; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10051655; DOI=10.1073/pnas.96.5.2408; RA Tan M.-W., Rahme L.G., Sternberg J.A., Tompkins R.G., Ausubel F.M.; RT "Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify RT P. aeruginosa virulence factors."; RL Proc. Natl. Acad. Sci. U.S.A. 96:2408-2413(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCBPP-PA14; RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90; RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.; RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is RT combinatorial."; RL Genome Biol. 7:R90.1-R90.14(2006). CC -!- FUNCTION: Involved in disulfide-bond formation. Acts by transferring CC its disulfide bond to other proteins (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. 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; AF116282; AAD22452.1; -; Genomic_DNA. DR EMBL; CP000438; ABJ14875.1; -; Genomic_DNA. DR RefSeq; WP_003096976.1; NC_008463.1. DR AlphaFoldDB; Q02DM0; -. DR BMRB; Q02DM0; -. DR SMR; Q02DM0; -. DR KEGG; pau:PA14_72450; -. DR PseudoCAP; PA14_72450; -. DR HOGENOM; CLU_088255_1_0_6; -. DR BioCyc; PAER208963:G1G74-6095-MONOMER; -. DR Proteomes; UP000000653; Chromosome. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProtKB-ARBA. DR CDD; cd03019; DsbA_DsbA; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 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 PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1. DR PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1. DR Pfam; PF01323; DSBA; 1. DR PIRSF; PIRSF001488; Tdi_protein; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00194; THIOREDOXIN_1; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Disulfide bond; Periplasm; Redox-active center; Reference proteome; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..211 FT /note="Thiol:disulfide interchange protein DsbA" FT /id="PRO_0000271730" FT DOMAIN 23..203 FT /note="Thioredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT DISULFID 56..59 FT /note="Redox-active" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691" FT CONFLICT 209 FT /note="Missing (in Ref. 1)" FT /evidence="ECO:0000305" SQ SEQUENCE 211 AA; 23375 MW; A994F93CC8E8C9F6 CRC64; MRNLILTAML AMASLFGMAA QADDYTAGKE YVELSSPVPV SQPGKIEVVE LFWYGCPHCY AFEPTIVPWS EKLPADVHFV RLPALFGGIW NVHGQMFLTL ESMGVEHDVH NAVFEAIHKE HKKLATPEEM ADFLAGKGVD KEKFLSTYNS FAIKGQMEKA KKLAMAYQVT GVPTMVVNGK YRFDIGSAGG PEETLKLADY LIEKERAAAK K //