ID A0A1V4B2G5_9PAST Unreviewed; 174 AA.
AC A0A1V4B2G5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Thiol:disulfide interchange protein DsbE {ECO:0000313|EMBL:STO59912.1};
GN Name=dsbE_2 {ECO:0000313|EMBL:STO59912.1};
GN ORFNames=NCTC1659_01177 {ECO:0000313|EMBL:STO59912.1};
OS Canicola haemoglobinophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Canicola.
OX NCBI_TaxID=733 {ECO:0000313|EMBL:STO59912.1, ECO:0000313|Proteomes:UP000254329};
RN [1] {ECO:0000313|EMBL:STO59912.1, ECO:0000313|Proteomes:UP000254329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC1659 {ECO:0000313|EMBL:STO59912.1,
RC ECO:0000313|Proteomes:UP000254329};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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; UGHF01000001; STO59912.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4B2G5; -.
DR STRING; 733.B0186_03350; -.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000254329; 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: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 Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000254329}.
FT DOMAIN 34..171
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 174 AA; 19483 MW; 88A89CB501931233 CRC64;
MSRKLMFIPL ILILAVCAML LLGLQQDPKK IASALIGKPV PEFSQADLFN PTKQLSNQNL
PNEVFLINVW GSWCEYCKQE HPILMELAQQ GIKIVGLNYR DKPQSAVAML ERMGNPFVLV
VNDSKGTLAM KLGVDGAPET YIVDKHGVIR YRHSGAFDPE LVQKVILPEL AKWK
//
