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Database: UniProt
Entry: Q5WYL4_LEGPL
LinkDB: Q5WYL4_LEGPL
Original site: Q5WYL4_LEGPL 
ID   Q5WYL4_LEGPL            Unreviewed;       586 AA.
AC   Q5WYL4;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   Name=dsbD {ECO:0000313|EMBL:CAH14956.1};
GN   Synonyms=lidC {ECO:0000313|EMBL:CAH14956.1};
GN   OrderedLocusNames=lpl0722 {ECO:0000313|EMBL:CAH14956.1};
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH14956.1, ECO:0000313|Proteomes:UP000002517};
RN   [1] {ECO:0000313|EMBL:CAH14956.1, ECO:0000313|Proteomes:UP000002517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens {ECO:0000313|EMBL:CAH14956.1,
RC   ECO:0000313|Proteomes:UP000002517};
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA   Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of host
RT   cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CR628337; CAH14956.1; -; Genomic_DNA.
DR   RefSeq; WP_011214898.1; NC_006369.1.
DR   AlphaFoldDB; Q5WYL4; -.
DR   KEGG; lpf:lpl0722; -.
DR   LegioList; lpl0722; -.
DR   HOGENOM; CLU_014657_3_0_6; -.
DR   Proteomes; UP000002517; 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   CDD; cd02953; DsbDgamma; 1.
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; IPR035671; DsbD_gamma.
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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..586
FT                   /note="Thioredoxin domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004263823"
FT   TRANSMEM        174..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..354
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          444..585
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   586 AA;  63988 MW;  0B49B34ED7EECA96 CRC64;
     MKKWLLFSLL FLTSLCVHAE PLPASEVFKV SVKKIDPNTF AIQWNILPKY FLYSDRIQLN
     SDNDDIAQLG ALRLPTPLTK TDKQGRTFKV YRNQLNLPVG VLGITPGETI VNLRFQGCAD
     DGFCYPPEVK QIKLAIDDKL ALSQVDLETF HAPEATPLEK PQQDIADIFA NHNWIMILLI
     FYGFGLLLSF TPCILPMVPV LSGIIVGHGK TATTKKAFFL SLSYVLSMSV TYAVVGAVVA
     LLGANLQISM QSPWAISLFS LIFVLLALSM FGFYEFKLPD AWQSKIVGSS REQRGGHYLG
     AAIMGCLSTL ILSPCVTAPL IGVLTYIAQT GNVLLGSVTL FTLSLGMGTP LLLIGTSAGK
     WLPETGSWMN AVKAFFGILL LAVAIYLMAR ILPAGLVMGL WACLLIFSGI YSGALTKSNT
     NQEKLCQGIG IILLTYGLLI LIGASMGSSN PLQPLANLQA APIVSNAFES AKAQSVKSVE
     LAIKQAFGKP VMLDFYADWC ASCKVMENTT FKDPRVQKAL SHFIVIKVDV TANNKNDRAL
     MQHFRVVAPP TFIFFNAQGI QLNNLKRVGE LNADEFMQTI KNIDAN
//
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