ID A0A397PA48_9SPHN Unreviewed; 262 AA.
AC A0A397PA48;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Thiol-disulfide isomerase/thioredoxin {ECO:0000313|EMBL:RIA46446.1};
GN ORFNames=DFR49_0988 {ECO:0000313|EMBL:RIA46446.1};
OS Hephaestia caeni.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Hephaestia.
OX NCBI_TaxID=645617 {ECO:0000313|EMBL:RIA46446.1, ECO:0000313|Proteomes:UP000266568};
RN [1] {ECO:0000313|EMBL:RIA46446.1, ECO:0000313|Proteomes:UP000266568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25527 {ECO:0000313|EMBL:RIA46446.1,
RC ECO:0000313|Proteomes:UP000266568};
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 (AUG-2018) 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:RIA46446.1}.
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DR EMBL; QXDC01000002; RIA46446.1; -; Genomic_DNA.
DR RefSeq; WP_030091394.1; NZ_QXDC01000002.1.
DR AlphaFoldDB; A0A397PA48; -.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000266568; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0016853; F:isomerase 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; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:RIA46446.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000266568};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 126..262
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 262 AA; 27641 MW; FC8FCEA0CF69A868 CRC64;
MIAIGPLALA LERLFAILGI IAFLAAANWI GRRRGVDCDT AAWRALLAGL VAARAGFVAQ
NWHAFAIEPA TILYVWQGGF SPLPGLVTAA IVLGVSLRRS RALAPLTLVF AGCVAVTSGA
TAAALASAQR PLPQGIVLQS LDSGTSLLDD RRGKPFVVNL WATWCPPCQR EMPMMVVEAA
HSAVPILLVN QGEDADNVRA WLDSKRLEAA HVHLDRDLRI AAATGSAGLP ATLFVDSKGV
IRALHVGEIS RAALLAGLRD LK
//
