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Database: UniProt
Entry: A0A0R2H5P2_9LACO
LinkDB: A0A0R2H5P2_9LACO
Original site: A0A0R2H5P2_9LACO 
ID   A0A0R2H5P2_9LACO        Unreviewed;       175 AA.
AC   A0A0R2H5P2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Redoxin domain-containing protein {ECO:0000313|EMBL:KRN44900.1};
GN   ORFNames=IV41_GL001956 {ECO:0000313|EMBL:KRN44900.1};
OS   Limosilactobacillus ingluviei.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN44900.1, ECO:0000313|Proteomes:UP000051639};
RN   [1] {ECO:0000313|EMBL:KRN44900.1, ECO:0000313|Proteomes:UP000051639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN44900.1,
RC   ECO:0000313|Proteomes:UP000051639};
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   -!- 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:KRN44900.1}.
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DR   EMBL; JQBA01000008; KRN44900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2H5P2; -.
DR   STRING; 1203076.GCA_000312405_00179; -.
DR   PATRIC; fig|148604.4.peg.2018; -.
DR   eggNOG; COG2077; Bacteria.
DR   Proteomes; UP000051639; Unassembled WGS sequence.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR   CDD; cd03014; PRX_Atyp2cys; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR002065; TPX.
DR   PANTHER; PTHR43110; THIOL PEROXIDASE; 1.
DR   PANTHER; PTHR43110:SF1; THIOL PEROXIDASE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051639}.
FT   DOMAIN          28..175
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   175 AA;  19533 MW;  3753DEA2DEE7BADE CRC64;
     MLSNNEKEAT IVEVTINGEV RSLVGNPPAV GEEMPHFKVF DKNDEKIKTR FLFGKPTLIS
     VVPDINTSVC SIQTKKFNEE VDKYTGANFL TVSTNTIADQ QKWCAAENVE HMQLVSDHEE
     SFGYALKLLI PEEGILARSV WVMDAEGKIT YREICPEIVA EPDYDAAIAA LKQLL
//
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