ID A0A0S3QR86_THET7 Unreviewed; 262 AA.
AC A0A0S3QR86;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Thiol:disulfide interchange protein DsbC {ECO:0000313|EMBL:BAT70848.1};
DE EC=5.3.4.1 {ECO:0000313|EMBL:BAT70848.1};
GN ORFNames=TST_0038 {ECO:0000313|EMBL:BAT70848.1};
OS Thermosulfidibacter takaii (strain DSM 17441 / JCM 13301 / NBRC 103674 /
OS ABI70S6).
OC Bacteria; Aquificota; Aquificae; Aquificales.
OX NCBI_TaxID=1298851 {ECO:0000313|EMBL:BAT70848.1, ECO:0000313|Proteomes:UP000063234};
RN [1] {ECO:0000313|Proteomes:UP000063234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17441 / JCM 13301 / NBRC 103674 / ABI70S6
RC {ECO:0000313|Proteomes:UP000063234};
RX PubMed=29420286; DOI=10.1126/science.aao3407;
RA Nunoura T., Chikaraishi Y., Izaki R., Suwa T., Sato T., Harada T., Mori K.,
RA Kato Y., Miyazaki M., Shimamura S., Yanagawa K., Shuto A., Ohkouchi N.,
RA Fujita N., Takaki Y., Atomi H., Takai K.;
RT "A primordial and reversible TCA cycle in a facultatively
RT chemolithoautotrophic thermophile.";
RL Science 359:559-563(2018).
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; AP013035; BAT70848.1; -; Genomic_DNA.
DR RefSeq; WP_068548532.1; NZ_AP013035.1.
DR AlphaFoldDB; A0A0S3QR86; -.
DR STRING; 1298851.TST_0038; -.
DR KEGG; ttk:TST_0038; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000063234; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35272:SF3; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC; 1.
DR PANTHER; PTHR35272; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC-RELATED; 1.
DR Pfam; PF10411; DsbC_N; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:BAT70848.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000063234};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..262
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006616342"
FT DOMAIN 75..258
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 262 AA; 29697 MW; 091ABC6879392F37 CRC64;
MRYLVGFLAF LLLTVNSFGK VPEAVTAKVK KIVGKEAKIV GVEPLPIKGL YGVFLQGTRG
MGVIVVTEDG NYLILGKILK VQDINKPEDV IAEIAKKKRY LKPPKPKKVD MSKIDIKNSP
RIGKEEAPEI VLYFDPTCPF CKKELATLRE MEKKGEVAFY PKYFIVHGKT AKEKAIEAEC
IREAYGKEAY YDYLLEGKKP KKEAKCDKEA IKKRIERDIK EAKELGITGT PTWIYNKEMY
VGYRPESEVK RIIDKGKGSK VE
//