ID A0A1L9BMD1_9RHOB Unreviewed; 192 AA.
AC A0A1L9BMD1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Thiol:disulfide oxidoreductase DsbE {ECO:0000313|EMBL:OJH43441.1};
GN ORFNames=IE00_16810 {ECO:0000313|EMBL:OJH43441.1};
OS Paracoccus sp. SM22M-07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1520813 {ECO:0000313|EMBL:OJH43441.1, ECO:0000313|Proteomes:UP000183790};
RN [1] {ECO:0000313|EMBL:OJH43441.1, ECO:0000313|Proteomes:UP000183790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM22M-07 {ECO:0000313|EMBL:OJH43441.1,
RC ECO:0000313|Proteomes:UP000183790};
RA Carlos C., Ottoboni L.;
RT "Draft sequencing and comparative genomics of Paracoccus sp. SM22M-07
RT isolated from coral mucus: Insights into bacteria-host interactions.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000256|ARBA:ARBA00007758}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJH43441.1}.
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; JPKW01000014; OJH43441.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L9BMD1; -.
DR STRING; 1520813.IE00_16810; -.
DR Proteomes; UP000183790; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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 Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000183790};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..188
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 192 AA; 21347 MW; 258FDDFC3E73EB08 CRC64;
MSSKDNQEQR RRSGRPLMIL PILLFGLLGV VFYWGLWNND DRLPSTLIGR PIPEFALPPI
EGRQDGLASA NLLDQVSLVN VWASWCVPCR TENPLLVNLA EAGTVPIYGI NYKDNAEEAL
GFLEELGDPF TRIGADRSGR VAIDWGVYGV PETYIIDAEG RIAYKHVGPF DQASLEEDIL
PVVRRLQAES DP
//
