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Database: UniProt
Entry: Q1MR89_LAWIP
LinkDB: Q1MR89_LAWIP
Original site: Q1MR89_LAWIP 
ID   Q1MR89_LAWIP            Unreviewed;       612 AA.
AC   Q1MR89;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Uncharacterized protein predicted to be involved in C-type cytochrome biogenesis {ECO:0000313|EMBL:CAJ54487.1};
GN   Name=dsbD {ECO:0000313|EMBL:CAJ54487.1};
GN   OrderedLocusNames=LI0433 {ECO:0000313|EMBL:CAJ54487.1};
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54487.1, ECO:0000313|Proteomes:UP000002430};
RN   [1] {ECO:0000313|EMBL:CAJ54487.1, ECO:0000313|Proteomes:UP000002430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54487.1,
RC   ECO:0000313|Proteomes:UP000002430};
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the causative
RT   agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AM180252; CAJ54487.1; -; Genomic_DNA.
DR   RefSeq; WP_011526517.1; NC_008011.1.
DR   AlphaFoldDB; Q1MR89; -.
DR   STRING; 363253.LI0433; -.
DR   KEGG; lip:LI0433; -.
DR   eggNOG; COG4232; Bacteria.
DR   HOGENOM; CLU_014657_1_2_7; -.
DR   OrthoDB; 9811036at2; -.
DR   Proteomes; UP000002430; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR028250; DsbDN.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR32234:SF3; SUPPRESSION OF COPPER SENSITIVITY PROTEIN; 1.
DR   PANTHER; PTHR32234; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD; 1.
DR   Pfam; PF02683; DsbD; 1.
DR   Pfam; PF11412; DsbD_N; 1.
DR   Pfam; PF00085; Thioredoxin; 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   Reference proteome {ECO:0000313|Proteomes:UP000002430};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        223..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        341..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        409..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        470..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          488..609
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   612 AA;  68451 MW;  2B0433F69480ED54 CRC64;
     MRQYRIIYLL LFYFIFCLSI SHPVAADITY SPLDVKFAYA LDTGTSPETV IIKMVLTVDD
     NYYTYTHNEK EGLPTKVVLQ NSSGTILQSR IFYPEGEIHE DVSSGISIKK VYSGEFPIFL
     QVQRDALTPE SEVQLSLLLC SSKHCMPVNR TIPITLPNPL PSIDEVPWED TYLLYTNPVV
     HTAESEHLID STEQTTDIAE SLFPWDLHPR YFQSGLEPTR IELALLFGFL AGLILNIMPC
     VLPVLTLKFS FILSHLGYKG EHCFRYVREQ NLLFAAGILS WFVMLALGVE VLELAWGGFF
     QSVPVVYGLM LIVFILALSL FGFFTLPIID FKIETTSFPR IQAYFTGVMT TLLATPCSGP
     LLGGVLGWAV LQPFYIIFIV FLATGLGMSL PYIIFAFKPQ AIRFLPRPGA WCGTLEQLVG
     FFLLGTTIYL LSILPETMLI QAIVTLLIAA FAVWCWGVLG GLSVSSTQRV VVGVVVSCMI
     AMSVWWSFHP AEKAHWLSYS DTKFRKELGL TPMLVEFTAD WCPTCKLLEK TVLTTSFLEQ
     LVNEYGIKLI KVDLTNKHSE AEALLRALGS VSIPVTAIFP SGEKANQPLV LRDVYTSEQL
     EKALQLAIKS SE
//
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