DSBA_PSEAE
ID DSBA_PSEAE Reviewed; 211 AA.
AC P0C2B2; P95460;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Thiol:disulfide interchange protein DsbA;
DE Flags: Precursor;
GN Name=dsbA; OrderedLocusNames=PA5489;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RA Leipelt M., Schneidinger B., Jaeger K.-E.;
RT "Cloning and sequencing of a dsbA-homologous gene from Pseudomonas
RT aeruginosa.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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}.
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DR EMBL; U84726; AAB41795.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08874.1; -; Genomic_DNA.
DR PIR; H82960; H82960.
DR RefSeq; NP_254176.1; NC_002516.2.
DR RefSeq; WP_003096976.1; NZ_QZGE01000012.1.
DR PDB; 2MBT; NMR; -; A=23-211.
DR PDB; 3H93; X-ray; 1.50 A; A=23-211.
DR PDB; 4ZL7; X-ray; 1.92 A; A=22-211.
DR PDB; 4ZL8; X-ray; 1.40 A; A=22-211.
DR PDB; 4ZL9; X-ray; 1.70 A; A=22-211.
DR PDB; 5DCH; X-ray; 1.45 A; A=22-211.
DR PDB; 5TLQ; NMR; -; A=23-211.
DR PDBsum; 2MBT; -.
DR PDBsum; 3H93; -.
DR PDBsum; 4ZL7; -.
DR PDBsum; 4ZL8; -.
DR PDBsum; 4ZL9; -.
DR PDBsum; 5DCH; -.
DR PDBsum; 5TLQ; -.
DR AlphaFoldDB; P0C2B2; -.
DR BMRB; P0C2B2; -.
DR SMR; P0C2B2; -.
DR STRING; 287.DR97_2867; -.
DR PaxDb; P0C2B2; -.
DR PRIDE; P0C2B2; -.
DR DNASU; 877731; -.
DR EnsemblBacteria; AAG08874; AAG08874; PA5489.
DR GeneID; 877731; -.
DR KEGG; pae:PA5489; -.
DR PATRIC; fig|208964.12.peg.5754; -.
DR PseudoCAP; PA5489; -.
DR HOGENOM; CLU_088255_1_0_6; -.
DR InParanoid; P0C2B2; -.
DR OMA; EVVEFFW; -.
DR PhylomeDB; P0C2B2; -.
DR BioCyc; PAER208964:G1FZ6-5616-MON; -.
DR BRENDA; 1.8.4.2; 5087.
DR EvolutionaryTrace; P0C2B2; -.
DR Proteomes; UP000002438; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..211
FT /note="Thiol:disulfide interchange protein DsbA"
FT /id="PRO_0000034262"
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"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:4ZL8"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3H93"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:4ZL8"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 106..118
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:4ZL8"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 151..167
FT /evidence="ECO:0007829|PDB:4ZL8"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:4ZL8"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:4ZL8"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:4ZL8"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:4ZL8"
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
