ID A0A1H7RLU2_STIAU Unreviewed; 469 AA.
AC A0A1H7RLU2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Thiol:disulfide interchange protein DsbD {ECO:0000313|EMBL:SEL61105.1};
GN ORFNames=SAMN05444354_10796 {ECO:0000313|EMBL:SEL61105.1};
OS Stigmatella aurantiaca.
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=41 {ECO:0000313|EMBL:SEL61105.1, ECO:0000313|Proteomes:UP000182719};
RN [1] {ECO:0000313|Proteomes:UP000182719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17044 {ECO:0000313|Proteomes:UP000182719};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FOAP01000007; SEL61105.1; -; Genomic_DNA.
DR RefSeq; WP_075007151.1; NZ_FOAP01000007.1.
DR AlphaFoldDB; A0A1H7RLU2; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000182719; Unassembled WGS sequence.
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:UP000182719};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 232..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..288
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..469
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 469 AA; 48686 MW; 0756559FF66A3343 CRC64;
MKKVGILAAV CGFAVLFVPW LLPTGPNAGL DASQFLETGS LAMGAAIVFA GGLLTALTPC
VYPLIPITVS IFGARQAEGR GKALLLTSSY IIGMGVVFSG LGVLAAKTGQ AFGSLLGHPG
VVLGLAVFLL VLATSMFGAF ELELPSSVQT RLSTVGGAGV AGAFLMGSVS GFLAAPCTGP
VLTGLLAFVA KTANTTLGAG LLFIYALGIG VPFFLIGVFT VRLPRGGVWM EWVKSVLGIV
LVALAFNYVK DAFPAVGSAV KGMAQELGRV PGAFIAAVLA GVGVLVGAIH RSFKSDARQF
ALKGVGVTLV VLALVSRVSA LDAAPTGALW VQLGWAEPPQ APTFQWHHVM PAKEATFSPA
AFEEALGRAR AEGRPVMIDF FADWCAACKE LDRETYPSFE VIEESSRFLN IKIDATNSED
ALDALMERFG VEGLPTVAFI ASNGEPLAAP RVTGFLPPSP FVSELKKVR
//
