DSBC_SALTY
ID DSBC_SALTY Reviewed; 237 AA.
AC P55890;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Thiol:disulfide interchange protein DsbC;
DE Flags: Precursor;
GN Name=dsbC; OrderedLocusNames=STM3043;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174.
RC STRAIN=LT2;
RX PubMed=9370270; DOI=10.1016/s0378-1119(97)00299-0;
RA Hayes F., Lubetzki S.A., Sherratt D.J.;
RT "Salmonella typhimurium specifies a circular chromosome dimer resolution
RT system which is homologous to the Xer site-specific recombination system of
RT Escherichia coli.";
RL Gene 198:105-110(1997).
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.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL21918.1; -; Genomic_DNA.
DR EMBL; U92524; AAC45775.1; -; Genomic_DNA.
DR RefSeq; NP_461959.1; NC_003197.2.
DR RefSeq; WP_000745625.1; NC_003197.2.
DR PDB; 4I5Q; X-ray; 1.96 A; A/B=23-237.
DR PDB; 4ILF; X-ray; 2.00 A; A/B=23-237.
DR PDBsum; 4I5Q; -.
DR PDBsum; 4ILF; -.
DR AlphaFoldDB; P55890; -.
DR SMR; P55890; -.
DR STRING; 99287.STM3043; -.
DR PaxDb; P55890; -.
DR EnsemblBacteria; AAL21918; AAL21918; STM3043.
DR GeneID; 1254566; -.
DR KEGG; stm:STM3043; -.
DR PATRIC; fig|99287.12.peg.3223; -.
DR HOGENOM; CLU_083593_0_0_6; -.
DR OMA; QMIVYKA; -.
DR PhylomeDB; P55890; -.
DR BioCyc; SENT99287:STM3043-MON; -.
DR Proteomes; UP000001014; 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 InterPro; IPR017937; Thioredoxin_CS.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54423; SSF54423; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Periplasm; Redox-active center;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..237
FT /note="Thiol:disulfide interchange protein DsbC"
FT /id="PRO_0000034274"
FT DISULFID 119..122
FT /note="Redox-active"
FT /evidence="ECO:0000255"
FT CONFLICT 44
FT /note="P -> A (in Ref. 2; AAC45775)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="N -> K (in Ref. 2; AAC45775)"
FT /evidence="ECO:0000305"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 83..93
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 152..161
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:4I5Q"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:4I5Q"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:4I5Q"
SQ SEQUENCE 237 AA; 25836 MW; 61F958FC1FE2ECC0 CRC64;
MKKRFMMFTL LAAVFSGVAH ADDAAIRQSL AKLGVQSTEI QASPVAGMKT VLTHSGVLYV
TDDGKHIIQG PMYDVSGAHP VNVTNKLLMS QLNALEKEMI VYKAPDEKHV ITVFTDITCG
YCHKLHEEMK DYNALGITVR YLAFPRQGLE SQAEQDMKSI WCAKDKNKAF DDAMAGKGVK
PASCDVNIAD HYALGVQLGV SGTPAIVLSN GYVVPGYQGP KEMKAFLDEH QKQTSGK
