ID Q2GHF8_EHRCR Unreviewed; 165 AA.
AC Q2GHF8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE SubName: Full=Thiol:disulfide oxidoreductase {ECO:0000313|EMBL:ABD44915.1};
GN OrderedLocusNames=ECH_0304 {ECO:0000313|EMBL:ABD44915.1};
OS Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=205920 {ECO:0000313|EMBL:ABD44915.1, ECO:0000313|Proteomes:UP000008320};
RN [1] {ECO:0000313|EMBL:ABD44915.1, ECO:0000313|Proteomes:UP000008320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC CRL-10679 / Arkansas {ECO:0000313|Proteomes:UP000008320};
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000256|ARBA:ARBA00007758}.
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DR EMBL; CP000236; ABD44915.1; -; Genomic_DNA.
DR RefSeq; WP_011452523.1; NC_007799.1.
DR AlphaFoldDB; Q2GHF8; -.
DR STRING; 205920.ECH_0304; -.
DR KEGG; ech:ECH_0304; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_4_5; -.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000008320; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000008320}.
FT DOMAIN 18..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 165 AA; 18895 MW; 8B73BAD130DAAC7B CRC64;
MRIIATALLV CFLTFTVILT KVLLNQNTIT DTTNRVVLPI LFTEDQVFDT NDLIGQPYIL
NVFASWCTTC QEEHSLWLEI AEKKTIKIYG INYLDTEYKV QEWLKKHGDP YTKIAKDYSG
KTGNVLGVTG VPETFIFDKN GKILLHIHGS VSRDTWENQI LKIIQ
//
