DSBH_CHLPN
ID DSBH_CHLPN Reviewed; 166 AA.
AC Q9Z6Y0; Q7AI22; Q7BWR2; Q7DE35;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Disulfide bond reductase DsbH;
DE Short=Disulfide reductase;
DE EC=1.8.-.-;
DE AltName: Full=Protein-disulfide reductase;
DE Flags: Precursor;
GN Name=dsbH; OrderedLocusNames=CPn_0926, CP_0940, CPj0926, CpB0958;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP STRUCTURE BY NMR OF 23-166 OF MUTANT GLY-63, FUNCTION, REDOX POTENTIAL,
RP GENE NAME, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=TW-183;
RX PubMed=18003611; DOI=10.1074/jbc.m707863200;
RA Mac T.T., von Hacht A., Hung K.C., Dutton R.J., Boyd D., Bardwell J.C.,
RA Ulmer T.S.;
RT "Insight into disulfide bond catalysis in Chlamydia from the structure and
RT function of DsbH, a novel oxidoreductase.";
RL J. Biol. Chem. 283:824-832(2008).
CC -!- FUNCTION: Catalyzes the reduction of disulfide bonds. May function in
CC reducing intermolecular disulfides between proteins and small molecules
CC in the periplasm, or keeping a specific subset of periplasmic proteins
CC reduced, or maintaining the periplasm of Chlamydia in a generally
CC reducing state. Seems to be unable to oxidize thiols into disulfides
CC and does not display disulfide bond isomerase activity.
CC {ECO:0000269|PubMed:18003611}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is -269.7 mV.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18003611}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:18003611}.
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DR EMBL; AE001363; AAD19064.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38723.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99134.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98887.1; -; Genomic_DNA.
DR PIR; D86606; D86606.
DR PIR; E72018; E72018.
DR RefSeq; NP_225121.1; NC_000922.1.
DR RefSeq; WP_010883561.1; NZ_LN847257.1.
DR PDB; 2JU5; NMR; -; A=23-166.
DR PDBsum; 2JU5; -.
DR AlphaFoldDB; Q9Z6Y0; -.
DR BMRB; Q9Z6Y0; -.
DR SMR; Q9Z6Y0; -.
DR STRING; 115711.CP_0940; -.
DR EnsemblBacteria; AAD19064; AAD19064; CPn_0926.
DR EnsemblBacteria; AAF38723; AAF38723; CP_0940.
DR GeneID; 45050982; -.
DR KEGG; cpa:CP_0940; -.
DR KEGG; cpj:CPj0926; -.
DR KEGG; cpn:CPn_0926; -.
DR KEGG; cpt:CpB0958; -.
DR PATRIC; fig|115713.3.peg.1007; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_090389_8_1_0; -.
DR OMA; GWCIRLQ; -.
DR OrthoDB; 1617952at2; -.
DR EvolutionaryTrace; Q9Z6Y0; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Oxidoreductase; Periplasm;
KW Redox-active center; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..166
FT /note="Disulfide bond reductase DsbH"
FT /id="PRO_0000415894"
FT DOMAIN 32..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT BINDING 73..74
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT DISULFID 72..75
FT /note="Redox-active"
FT /evidence="ECO:0000305"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2JU5"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2JU5"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2JU5"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2JU5"
FT HELIX 73..81
FT /evidence="ECO:0007829|PDB:2JU5"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2JU5"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:2JU5"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:2JU5"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:2JU5"
FT STRAND 128..135
FT /evidence="ECO:0007829|PDB:2JU5"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2JU5"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:2JU5"
SQ SEQUENCE 166 AA; 18903 MW; 032532AE8E1C5DDA CRC64;
MKFWLQGCAF VGCLLLTLPC CAARRRASGE NLQQTRPIAA ANLQWESYAE ALEHSKQDHK
PICLFFTGSD WCMWCIKMQD QILQSSEFKH FAGVHLHMVE VDFPQKNHQP EEQRQKNQEL
KAQYKVTGFP ELVFIDAEGK QLARMGFEPG GGAAYVSKVK SALKLR
