ID D1KBF4_9GAMM Unreviewed; 173 AA.
AC D1KBF4;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Thiol-disulfide isomerase {ECO:0000313|EMBL:EEZ80540.1};
GN ORFNames=Sup05_0366 {ECO:0000313|EMBL:EEZ80540.1};
OS uncultured Candidatus Thioglobus sp.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Thioglobus;
OC environmental samples.
OX NCBI_TaxID=655186 {ECO:0000313|EMBL:EEZ80540.1, ECO:0000313|Proteomes:UP000009383};
RN [1] {ECO:0000313|EMBL:EEZ80540.1, ECO:0000313|Proteomes:UP000009383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19900896; DOI=10.1126/science.1175309;
RA Walsh D.A., Zaikova E., Howes C.L., Song Y.C., Wright J.J., Tringe S.G.,
RA Tortell P.D., Hallam S.J.;
RT "Metagenome of a versatile chemolithoautotroph from expanding oceanic dead
RT zones.";
RL Science 326:578-582(2009).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004383}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004383}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004383}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000256|ARBA:ARBA00007758}.
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DR EMBL; GG729978; EEZ80540.1; -; Genomic_DNA.
DR AlphaFoldDB; D1KBF4; -.
DR STRING; 655186.Sup05_0366; -.
DR PATRIC; fig|655186.3.peg.1117; -.
DR Proteomes; UP000009383; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR CDD; cd03010; TlpA_like_DsbE; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR00385; dsbE; 1.
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; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytochrome c-type biogenesis {ECO:0000256|ARBA:ARBA00022748};
KW Isomerase {ECO:0000313|EMBL:EEZ80540.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000009383}.
FT DOMAIN 31..173
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 173 AA; 19543 MW; FA6F0CBBFBAC7FB0 CRC64;
MNKFLPLGLF VVLVGFLYVG LGLDPKKLPS PLIGKSFPDM EVEDFHTGEK YSTQDKLKTK
ISLVNVWASW CATCRAEHEM LMKIAKTNAV QMMGINYKDT KKDGTKFIDV LGNPYNLVIF
DQLGKLGLEL GVYATPETFL VDQDGVIRFK RIGEMTGRIW EKEVLPLVNQ LKI
//
