ID E0E2B8_9FIRM Unreviewed; 386 AA.
AC E0E2B8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Redoxin family protein {ECO:0000313|EMBL:EFM64934.1};
DE EC=1.11.1.15 {ECO:0000313|EMBL:EFM64934.1};
GN ORFNames=HMPREF0634_1248 {ECO:0000313|EMBL:EFM64934.1};
OS Peptostreptococcus stomatis DSM 17678.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=596315 {ECO:0000313|EMBL:EFM64934.1, ECO:0000313|Proteomes:UP000003244};
RN [1] {ECO:0000313|EMBL:EFM64934.1, ECO:0000313|Proteomes:UP000003244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17678 {ECO:0000313|EMBL:EFM64934.1,
RC ECO:0000313|Proteomes:UP000003244};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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:EFM64934.1}.
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DR EMBL; ADGQ01000035; EFM64934.1; -; Genomic_DNA.
DR AlphaFoldDB; E0E2B8; -.
DR STRING; 596315.HMPREF0634_1248; -.
DR eggNOG; COG0526; Bacteria.
DR Proteomes; UP000003244; 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; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
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; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:EFM64934.1};
KW Peroxidase {ECO:0000313|EMBL:EFM64934.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003244};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..386
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039271986"
FT DOMAIN 232..382
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 29..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 386 AA; 43032 MW; D2B7D357B8BD04C3 CRC64;
MSIMKKRALK GAAVLLTLCI TLGAVGCQKG EDKGKAKENQ SVTSEQAGMT TDAKGNNKFK
PADYTLPSKD EYTYEFLGLK FKLSDNIRKD IDGKNLAMLD DQSPVEKDLK YAMLTFNKMT
DEQKNAVIDK MGDGYEKWKS ELERVGTIGM FEKGMSEDEI SKITKCDTHK KLGESSDGKY
TYYISTKSGA KDNFAEEFNK TKVDIIEKKA RPENGFVLSE KKDLEGTEAF DKGSAKDLRN
LSTKDINGKE FTSKEFGKYD LTMVNVFATW CTACVKEIPD LVKVQNEMKS KGVNIVGVVT
DTVDDNGNNK EAIDKSKLIQ KKTKASYPFL MPDKSNFNGR LNGIQAMPET FFVDKNGNIV
GDTYSGAKTA SEWKQVIEKE LAKIKK
//
