ID A0A0R2FEJ7_9LACO Unreviewed; 106 AA.
AC A0A0R2FEJ7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Thioredoxin {ECO:0000256|ARBA:ARBA00020570, ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=FC75_GL001693 {ECO:0000313|EMBL:KRN23053.1};
OS Lacticaseibacillus camelliae DSM 22697 = JCM 13995.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423730 {ECO:0000313|EMBL:KRN23053.1, ECO:0000313|Proteomes:UP000050865};
RN [1] {ECO:0000313|EMBL:KRN23053.1, ECO:0000313|Proteomes:UP000050865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22697 {ECO:0000313|EMBL:KRN23053.1,
RC ECO:0000313|Proteomes:UP000050865};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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:KRN23053.1}.
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DR EMBL; AYZJ01000029; KRN23053.1; -; Genomic_DNA.
DR RefSeq; WP_054665174.1; NZ_BBAJ01000056.1.
DR AlphaFoldDB; A0A0R2FEJ7; -.
DR STRING; 1423730.FC75_GL001693; -.
DR PATRIC; fig|1423730.4.peg.1770; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000050865; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
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|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Isomerase {ECO:0000313|EMBL:KRN23053.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000050865};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..103
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 22
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 29
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 30
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 28..31
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 106 AA; 11874 MW; 2C1A61190578FB6C CRC64;
MVKVVSDQDF KQETDTGVTL TDFWATWCGP CKMQSPVIES LEKDRSDVKF TKMDVDQNPE
TPGAFGIMAI PTLIVKKDGE VVEKLVGYQT KDQLNNVLDK YTKTPA
//
