ID   DSBC_HAEIN              Reviewed;         229 AA.
AC   P45111;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Thiol:disulfide interchange protein DsbC;
DE   Flags: Precursor;
GN   Name=dsbC; Synonyms=xprA; OrderedLocusNames=HI_1213;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-229, SUBUNIT, AND DISULFIDE
RP   BOND.
RX   PubMed=15333920; DOI=10.1107/s0907444904014593;
RA   Zhang M., Monzingo A.F., Segatori L., Georgiou G., Robertus J.D.;
RT   "Structure of DsbC from Haemophilus influenzae.";
RL   Acta Crystallogr. D 60:1512-1518(2004).
CC   -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC       proteins. Acts by transferring its disulfide bond to other proteins and
CC       is reduced in the process. DsbC is reoxidized by a yet uncharacterized
CC       protein. Also acts as a disulfide isomerase (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15333920}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; L42023; AAC22866.1; -; Genomic_DNA.
DR   PIR; E64110; E64110.
DR   RefSeq; NP_439369.1; NC_000907.1.
DR   RefSeq; WP_005647404.1; NC_000907.1.
DR   PDB; 1T3B; X-ray; 2.50 A; A=19-229.
DR   PDBsum; 1T3B; -.
DR   AlphaFoldDB; P45111; -.
DR   SMR; P45111; -.
DR   STRING; 71421.HI_1213; -.
DR   EnsemblBacteria; AAC22866; AAC22866; HI_1213.
DR   KEGG; hin:HI_1213; -.
DR   PATRIC; fig|71421.8.peg.1265; -.
DR   eggNOG; COG1651; Bacteria.
DR   HOGENOM; CLU_083593_0_0_6; -.
DR   OMA; QMIVYKA; -.
DR   PhylomeDB; P45111; -.
DR   BioCyc; HINF71421:G1GJ1-1244-MON; -.
DR   EvolutionaryTrace; P45111; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR   Gene3D; 3.10.450.70; -; 1.
DR   InterPro; IPR033954; DiS-bond_Isoase_DsbC/G.
DR   InterPro; IPR018950; DiS-bond_isomerase_DsbC/G_N.
DR   InterPro; IPR009094; DiS-bond_isomerase_DsbC/G_N_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF10411; DsbC_N; 1.
DR   Pfam; PF13098; Thioredoxin_2; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   SUPFAM; SSF54423; SSF54423; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Periplasm; Redox-active center;
KW   Reference proteome; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000250"
FT   CHAIN           19..229
FT                   /note="Thiol:disulfide interchange protein DsbC"
FT                   /id="PRO_0000034276"
FT   DISULFID        116..119
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:15333920"
FT   TURN            21..23
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           24..28
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   TURN            73..75
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           81..90
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           91..95
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           117..123
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           126..131
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   STRAND          134..140
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           149..159
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           163..171
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           184..195
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   STRAND          202..204
FT                   /evidence="ECO:0007829|PDB:1T3B"
FT   HELIX           217..226
FT                   /evidence="ECO:0007829|PDB:1T3B"
SQ   SEQUENCE   229 AA;  25351 MW;  AF0F08AFC0FD08E6 CRC64;
     MKKIFTALLC VAAANAMADD AAIKRKLQSF NISNIVIKSS PISGIKTAVT DQGILYVSED
     GKYLFEGKLY ELTNNGPVDV AGKILVDKLN SYKDEMIVYP AKNEKHVVTV FMDITCHYCH
     LLHQQLKEYN DLGITVRYLA FPRAGMNNQT AKQMEAIWTA KDPVFALNEA EKGNLPKEVK
     TPNIVKKHYE LGIQFGVRGT PSIVTSTGEL IGGYLKPADL LRALEETAQ