ID A0A106BR21_THIDE Unreviewed; 236 AA.
AC A0A106BR21;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=ABW22_06580 {ECO:0000313|EMBL:KVW97060.1};
OS Thiobacillus denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=36861 {ECO:0000313|EMBL:KVW97060.1, ECO:0000313|Proteomes:UP000064243};
RN [1] {ECO:0000313|EMBL:KVW97060.1, ECO:0000313|Proteomes:UP000064243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RG {ECO:0000313|EMBL:KVW97060.1,
RC ECO:0000313|Proteomes:UP000064243};
RX PubMed=26712544;
RA Harrold Z.R., Skidmore M.L., Hamilton T.L., Desch L., Amada K.,
RA van Gelder W., Glover K., Roden E.E., Boyd E.S.;
RT "Aerobic and Anaerobic Thiosulfate Oxidation by a Cold-Adapted, Subglacial
RT Chemoautotroph.";
RL Appl. Environ. Microbiol. 82:1486-1495(2015).
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. {ECO:0000256|RuleBase:RU364038}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU364038}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbC subfamily.
CC {ECO:0000256|ARBA:ARBA00009813, ECO:0000256|RuleBase:RU364038}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVW97060.1}.
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DR EMBL; LDUG01000018; KVW97060.1; -; Genomic_DNA.
DR RefSeq; WP_059753568.1; NZ_LDUG01000018.1.
DR AlphaFoldDB; A0A106BR21; -.
DR STRING; 1123392.GCA_000376425_01952; -.
DR PATRIC; fig|36861.3.peg.789; -.
DR OrthoDB; 12976at2; -.
DR Proteomes; UP000064243; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR CDD; cd03020; DsbA_DsbC_DsbG; 1.
DR Gene3D; 3.10.450.70; Disulphide bond isomerase, DsbC/G, N-terminal; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 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 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; PF13098; Thioredoxin_2; 1.
DR SUPFAM; SSF54423; DsbC/DsbG N-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU364038};
KW Redox-active center {ECO:0000256|RuleBase:RU364038};
KW Reference proteome {ECO:0000313|Proteomes:UP000064243};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 21..236
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010003055"
FT DOMAIN 26..79
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 107..231
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 236 AA; 25842 MW; E81CD1B91E7EB879 CRC64;
MKLAPLALAA TLMFAATAQA NESVIRKTLT QQFPGASIAS VQKTPYSGLF EVYLDGQLIY
VDAKAQYVFT GDVIDLKNRS NLTQARLNKL QAVKWDTLPL NNALKTVKGN GARKLVVFSD
VDCPYCRKFE AELTRVDNIT VYTFLYPIEG LHPKAVQTSK QIWCAPDRNK AWEDYTTKNV
VPNNDGKCAN PVDATIALGN KLKVSGTPTL IFANGQRVPG MVPAAQLEKL LAAHAK
//