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Database: UniProt
Entry: G5K1E0_9STRE
LinkDB: G5K1E0_9STRE
Original site: G5K1E0_9STRE 
ID   G5K1E0_9STRE            Unreviewed;       151 AA.
AC   G5K1E0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Glutathione peroxidase {ECO:0000313|EMBL:EHI70055.1};
GN   ORFNames=STRIC_2197 {ECO:0000313|EMBL:EHI70055.1};
OS   Streptococcus ictaluri 707-05.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764299 {ECO:0000313|EMBL:EHI70055.1, ECO:0000313|Proteomes:UP000003330};
RN   [1] {ECO:0000313|EMBL:EHI70055.1, ECO:0000313|Proteomes:UP000003330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=707-05 {ECO:0000313|EMBL:EHI70055.1,
RC   ECO:0000313|Proteomes:UP000003330};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
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:EHI70055.1}.
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DR   EMBL; AEUX02000005; EHI70055.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5K1E0; -.
DR   STRING; 764299.STRIC_2197; -.
DR   eggNOG; COG0526; Bacteria.
DR   OrthoDB; 25753at2; -.
DR   Proteomes; UP000003330; Unassembled WGS sequence.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   CDD; cd02966; TlpA_like_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:EHI70055.1};
KW   Peroxidase {ECO:0000313|EMBL:EHI70055.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003330};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..151
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003479501"
FT   DOMAIN          32..151
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   151 AA;  17095 MW;  6D2EDACC547F46E6 CRC64;
     MIKIIKKLLL VVPLFLLVAC SNDESISKNP GLAAGDQVPN VTLRNQEGDD MPLSDFKGKK
     VYINVWASWC GPCRHEMPDL EKVYQEVKDQ KDLVFISLTS PGDKAFNNQN PADQSKETIL
     EVAKEEGINY PIYFDTKDNA MKRQHFSVQH L
//
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