ID A0A317CB17_9GAMM Unreviewed; 178 AA.
AC A0A317CB17;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=DsbE family thiol:disulfide interchange protein {ECO:0000313|EMBL:PWQ95824.1};
GN ORFNames=DKW60_14075 {ECO:0000313|EMBL:PWQ95824.1};
OS Leucothrix pacifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Leucothrix.
OX NCBI_TaxID=1247513 {ECO:0000313|EMBL:PWQ95824.1, ECO:0000313|Proteomes:UP000245539};
RN [1] {ECO:0000313|EMBL:PWQ95824.1, ECO:0000313|Proteomes:UP000245539}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 18388 {ECO:0000313|EMBL:PWQ95824.1,
RC ECO:0000313|Proteomes:UP000245539};
RA Choi A., Baek K.;
RT "Leucothrix arctica sp. nov., isolated from Arctic seawater.";
RL Submitted (MAY-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}.
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:PWQ95824.1}.
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DR EMBL; QGKM01000041; PWQ95824.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317CB17; -.
DR OrthoDB; 9799347at2; -.
DR Proteomes; UP000245539; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000245539};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..175
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 178 AA; 19696 MW; F91A8106C4F122B4 CRC64;
MKKGALIPLI IFAVLVVFLG IGLGLKPREV PSPFIGKAVP EFRLPELMKD GESIAPADLK
GEVWMLNVFA SWCVSCRAEH EVLSNFINAE KVMVLGLNYK DEPDNAKKWL GALGNPYQHI
AVDYDGKVGI DLGVYGVPET FVVDKKGIVR HKVTGPVYQE TVRDTLLPLV LKLREEKV
//
