ID Q1D2G8_MYXXD Unreviewed; 506 AA.
AC Q1D2G8;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:ABF88490.1};
GN Name=dbsD {ECO:0000313|EMBL:ABF88490.1};
GN OrderedLocusNames=MXAN_4999 {ECO:0000313|EMBL:ABF88490.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF88490.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF88490.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000113; ABF88490.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1D2G8; -.
DR STRING; 246197.MXAN_4999; -.
DR EnsemblBacteria; ABF88490; ABF88490; MXAN_4999.
DR KEGG; mxa:MXAN_4999; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_3_1_7; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000002402; 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; 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; PF13899; Thioredoxin_7; 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:UP000002402};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 363..500
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 506 AA; 52504 MW; CFAA647B6FC48369 CRC64;
MPLQRSSPWP PACVYKGGLG ARSHARMDAK KLGVMAVLAG VAVAVVPWLL PTGPNANLDA
ARFLEAGSLA VGAAVVFAGG LLTALTPCVY PLIPITVSVF GARKTEGRGR ALLLTSSYIV
GMGVVFSALG VLAAKTGQAF GSMLGHPAVV TGLAVFLLLL ATSMFGAFEL ALPSSFQTKL
NAVGGAGVAG AFLMGSVSGF LAAPCTGPVL TGLLAFVAKS ANTTLGASLL FVYALGIGVP
FFLIGVFTVR LPRGGVWMEW VKSVLGIMLV ALAFSYLKDA FPWARDVVKG LGLHVGRVPG
AVIAALLVAV GVALGAVHRS FKEGAREFSF KALGVALVVA ALVLRGGALD GGPVGTLWVS
LGLAEPARAP AWQWHHVMPA KQATFSPEAF DQVLAQAKAE GRPVLIDFFA DWCAACKELD
RDTYPAQQVI SESDEGRFLN IKIDATNSED SLDALLERFG VEGLPTVAFI SPEGKVLTQP
RVTGFLAPSP FATEMKKARC TDANAC
//
