ID A0A495RCP2_9GAMM Unreviewed; 210 AA.
AC A0A495RCP2;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Thiol:disulfide interchange protein {ECO:0000256|PIRNR:PIRNR001488};
GN ORFNames=DES39_1638 {ECO:0000313|EMBL:RKS85129.1};
OS Orbus hercynius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Orbales; Orbaceae; Orbus.
OX NCBI_TaxID=593135 {ECO:0000313|EMBL:RKS85129.1, ECO:0000313|Proteomes:UP000278542};
RN [1] {ECO:0000313|EMBL:RKS85129.1, ECO:0000313|Proteomes:UP000278542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22228 {ECO:0000313|EMBL:RKS85129.1,
RC ECO:0000313|Proteomes:UP000278542};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|PIRNR:PIRNR001488}.
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|PIRNR:PIRNR001488}.
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:RKS85129.1}.
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DR EMBL; RBWY01000003; RKS85129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A495RCP2; -.
DR OrthoDB; 9784896at2; -.
DR Proteomes; UP000278542; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR CDD; cd03019; DsbA_DsbA; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR023205; DsbA/DsbL.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR35891; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR PANTHER; PTHR35891:SF2; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBA; 1.
DR Pfam; PF13462; Thioredoxin_4; 1.
DR PIRSF; PIRSF001488; Tdi_protein; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|PIRNR:PIRNR001488};
KW Periplasm {ECO:0000256|PIRNR:PIRNR001488};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000278542};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..210
FT /note="Thiol:disulfide interchange protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019782632"
FT DOMAIN 5..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DISULFID 57..60
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR001488-1"
SQ SEQUENCE 210 AA; 24180 MW; 42295B3E0238701C CRC64;
MHNILKSLVI ALLFSLSYVA DAELIENQDY IVLNSQIAKD PSPQDKIEVI EFFSYGCPYC
DKLEPQIAQW LAQKPANVTF TRIAIPRKGK WNEYARLFYA LGMISPAEQD RITPLMYAAI
HKQKLSFEND DAIFSWAQRQ GINRKLLEKY YNSEVVSDKL KLAMELARSF GLKYVPSIYV
NHQYQLILDS SNQYQGAQDK LNELITISSK
//
