ID A0A385C4I3_9GAMM Unreviewed; 670 AA.
AC A0A385C4I3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Protein-disulfide reductase DsbD {ECO:0000313|EMBL:AXQ22621.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:AXQ22621.1};
GN Name=dsbD {ECO:0000313|EMBL:AXQ22621.1};
GN ORFNames=BEN71_11290 {ECO:0000313|EMBL:AXQ22621.1};
OS Acinetobacter wuhouensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1879050 {ECO:0000313|EMBL:AXQ22621.1, ECO:0000313|Proteomes:UP000257257};
RN [1] {ECO:0000313|EMBL:AXQ22621.1, ECO:0000313|Proteomes:UP000257257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCHA60 {ECO:0000313|EMBL:AXQ22621.1,
RC ECO:0000313|Proteomes:UP000257257};
RX PubMed=30117799; DOI=10.1099/ijsem.0.002963;
RA Hu Y., Feng Y., Qin J., Radolfova-Krizova L., Maixnerova M., Zhang X.,
RA Nemec A., Zong Z.;
RT "Acinetobacter wuhouensis sp. nov., isolated from hospital sewage.";
RL Int. J. Syst. Evol. Microbiol. 68:3212-3216(2018).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP031716; AXQ22621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A385C4I3; -.
DR STRING; 1879050.GCA_001696605_00432; -.
DR KEGG; awu:BEN71_11290; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000257257; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; IEA:UniProtKB-EC.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR PANTHER; PTHR32234:SF0; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF11412; DsbD_N; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AXQ22621.1};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..670
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017212416"
FT TRANSMEM 262..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 423..444
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 456..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 511..528
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 532..667
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 134..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 73875 MW; A5B7DA736084282E CRC64;
MSFKKLISIG CFTLLGLSSI SHANSDFLPP DQAFQLSVES ISNQKAQLKW TIAPHYYLYH
DQFKVNLEHK SVPLHLPKGQ IKDDPTFGKT EVHYEQVSTQ INVKPNADYQ VLYQGCSADG
LCYPLQRKTI STDANGLFPQ NSSSANRLLN RQSNDNNSLE QSSSNKVKVQ DAKQDPIKND
SILAPVEDKK LPDAPVKLDS INSPASSEAT DQNPTSNVIA TNSNESANVA QSIEKNSNID
NTTSLQWNDD QSFFKLLSKD SLFLNLLVFF GLGILLAFLP CSLPLIPILS GIIIKNAKGY
KAVAIALSFV ISMAVIYAIM GIVVAEIGYS FQRWFQSPWI VSLFAVLFVV LALNLFGLYQ
LNLPQFITNK LSNLQNNQKA GTILGAVVMG ALSALIVGPC MSAPLAGALL FVSQSQSAVL
GGLYLFILGL GIGLPLFIAS VFGSRLLPKP GKWMDRIKVS FGFIMLMVAL YFIRPMLSTT
IYSALFALLC LVLAIYLFNA LRDSEKVLNK VILALIAVVS LVASFWNIQQ SYAAYQTQYS
QTAHLTWNKV STAEQLNTAL NDAKLIGKPI IIDVYADWCV ACQPIEKEVF PQVEVQTALK
DFTLIQLDLT KYNESQDLIL KQHEILGPPT MLFLNANAQE IRGLRFTGTF NAKQLIQQTA
KIKTQLNHSP
//
