ID Q0BVI6_GRABC Unreviewed; 236 AA.
AC Q0BVI6;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 89.
DE SubName: Full=Thiol:disulfide interchange protein tlpA {ECO:0000313|EMBL:ABI61166.2};
GN OrderedLocusNames=GbCGDNIH1_0268 {ECO:0000313|EMBL:ABI61166.2};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61166.2, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61166.2, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000394; ABI61166.2; -; Genomic_DNA.
DR AlphaFoldDB; Q0BVI6; -.
DR STRING; 391165.GbCGDNIH1_0268; -.
DR KEGG; gbe:GbCGDNIH1_0268; -.
DR eggNOG; COG0526; Bacteria.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd03010; TlpA_like_DsbE; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..233
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 236 AA; 25460 MW; 120A6C207A10F0F2 CRC64;
MAGCAGHGDW WMPVPDRPPV TCGCPCPQPC RSRLIAPEES NSMIPSPPPS RPVWTRRLLL
SVPLVLAVAA GAAFLGMLHG MEDGHFDPRG VPSPLIGKPV PVFDLPAQTP SPEGFTSAAL
TQHGHPVLVN FFASWCVPCK IEQPALMALK QRGIALWGIA YKDKPEAAAA MLKADGNPYQ
RIARDAAGGT AIDWGVYGVP ETYFVDPKGI VRWKWAGPLT EQVIKDQIEP LLKAYP
//