ID A0A0S2TEV2_9GAMM Unreviewed; 249 AA.
AC A0A0S2TEV2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|RuleBase:RU364038};
GN ORFNames=Tel_11455 {ECO:0000313|EMBL:ALP53702.1};
OS Candidatus Tenderia electrophaga.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Tenderia.
OX NCBI_TaxID=1748243 {ECO:0000313|EMBL:ALP53702.1, ECO:0000313|Proteomes:UP000055136};
RN [1] {ECO:0000313|EMBL:ALP53702.1, ECO:0000313|Proteomes:UP000055136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRL1 {ECO:0000313|EMBL:ALP53702.1};
RA Eddie B.J., Malanoski A.P., Wang Z., Hall R.J., Oh S.D., Heiner C., Lin B.,
RA Strycharz-Glaven S.M.;
RT "Description of Candidatus Tenderia electrophaga gen. nov, sp. nov., an
RT Uncultivated Electroautotroph from a Biocathode Enrichment.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP013099; ALP53702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S2TEV2; -.
DR STRING; 1748243.Tel_11455; -.
DR KEGG; tee:Tel_11455; -.
DR Proteomes; UP000055136; Chromosome.
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:UP000055136};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU364038}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT CHAIN 21..249
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|RuleBase:RU364038"
FT /id="PRO_5010001544"
FT DOMAIN 34..85
FT /note="Disulphide bond isomerase DsbC/G N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10411"
FT DOMAIN 118..245
FT /note="Thioredoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF13098"
SQ SEQUENCE 249 AA; 26915 MW; 345CFBA87F43554B CRC64;
MKQIYGIAFI LLFSAQSASA EDTPSSLNFA NVERTVHKAL PGTHITSIQP SVLPGLVEII
AGPNVLYADP TGHYLVVGSI YDMQTATDLT AQRKREVAQT ARIKWDDLPL ETAVKYGGQG
PTKLAVFFDP DCPWCKRLHE QLSALDDVEV YAIMYPVESL HAGAKNKAAA ILCSSDPLQA
LNRVMAGKDL PAVSDPTCLA RNNAAIDRIE AFARSHDIHG TPTLIAPDGR VRPGFLQAKP
LKAWLDASS
//
