ID Q5FG23_EHRRG Unreviewed; 166 AA.
AC Q5FG23;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE SubName: Full=Thiol:disulfide interchange protein dsb {ECO:0000313|EMBL:CAI28170.1};
GN Name=dsbE {ECO:0000313|EMBL:CAI28170.1};
GN OrderedLocusNames=ERGA_CDS_07180 {ECO:0000313|EMBL:CAI28170.1};
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409 {ECO:0000313|EMBL:CAI28170.1, ECO:0000313|Proteomes:UP000000533};
RN [1] {ECO:0000313|EMBL:CAI28170.1, ECO:0000313|Proteomes:UP000000533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel {ECO:0000313|EMBL:CAI28170.1,
RC ECO:0000313|Proteomes:UP000000533};
RX PubMed=16547041; DOI=10.1128/JB.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000256|ARBA:ARBA00007758}.
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DR EMBL; CR925677; CAI28170.1; -; Genomic_DNA.
DR RefSeq; WP_011255795.1; NC_006831.1.
DR AlphaFoldDB; Q5FG23; -.
DR KEGG; erg:ERGA_CDS_07180; -.
DR HOGENOM; CLU_042529_19_4_5; -.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000000533; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
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 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 Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 18..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 166 AA; 18976 MW; 04122CB0381FC515 CRC64;
MKIFGTIFLI CFLMFVAIFT KTLLDKNTVP DVSSRIVLPL LYTEDKLLDT NELIGHPYIL
NVFASWCTTC QEEHGILLDI AKKQMIKIYG INYLDTEYKV KEWLKTNGNP YTEIAKDYSG
KVNSALGVTG VPETFIFDQH GKLILHIHGN LPENIWETQI LPLIQN
//
