ID L7UFG3_MYXSD Unreviewed; 480 AA.
AC L7UFG3;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:AGC46768.1};
GN OrderedLocusNames=MYSTI_05490 {ECO:0000313|EMBL:AGC46768.1};
OS Myxococcus stipitatus (strain DSM 14675 / JCM 12634 / Mx s8).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=1278073 {ECO:0000313|EMBL:AGC46768.1, ECO:0000313|Proteomes:UP000011131};
RN [1] {ECO:0000313|EMBL:AGC46768.1, ECO:0000313|Proteomes:UP000011131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14675 / JCM 12634 / Mx s8
RC {ECO:0000313|Proteomes:UP000011131};
RX PubMed=23516218; DOI=10.1128/genomeA.00100-13;
RA Huntley S., Kneip S., Treuner-Lange A., Sogaard-Andersen L.;
RT "Complete genome sequence of Myxococcus stipitatus strain DSM 14675, a
RT fruiting myxobacterium.";
RL Genome Announc. 1:E0010013-E0010013(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP004025; AGC46768.1; -; Genomic_DNA.
DR RefSeq; WP_015351024.1; NC_020126.1.
DR AlphaFoldDB; L7UFG3; -.
DR STRING; 1278073.MYSTI_05490; -.
DR KEGG; msd:MYSTI_05490; -.
DR PATRIC; fig|1278073.3.peg.5568; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_1_7; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000011131; 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 InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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; PF13098; Thioredoxin_2; 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 Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 348..474
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 480 AA; 49788 MW; 9E12BEC78EAFD203 CRC64;
MNGKKLGVLA VLAGVAVVVV PWLLPTGPST ELDAARFLES GSLFLGAAIV FAGGLLTALT
PCVYPLIPIT VSVFGARKAE SRGKAMLLTT SYIVGMGVVF SALGILAAKT GQAFGSMLGH
PAVVTGLAVF LLLLASSMFG AFELALPSGL QNRLNSVGGA GVAGAFLMGS VSGFLAAPCT
GPVLTGLLAF VAKTANTTLG ATLLFIYALG IGVPFFILGV STVRLPKSGV WMEWVKSVLG
IVLVALAFNY LKDASPWARD VVKAAGAELG RVPGAALAGV LAVVGVLVGA VHRSFKEGSR
EFSLKAVGVV LVVVALVIRG GALDAGPVGS LWVRMGVAEP PRAPSWQWHH VMPAKKATFS
PADFEKVLAQ AKAEGRPVLI DFFADWCAAC KELDRETYPA QEVISQSSEG QFLNIKIDAT
NSEDALDALM ERFGVEGLPT VAFVSQDGTV LTRPRITGFL EPTPFAAEMR KARCTDGGSC
//
