ID A0A0N9UY61_SPHMC Unreviewed; 637 AA.
AC A0A0N9UY61;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:ALH79969.1};
GN ORFNames=AN936_06185 {ECO:0000313|EMBL:ALH79969.1};
OS Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH79969.1, ECO:0000313|Proteomes:UP000058074};
RN [1] {ECO:0000313|EMBL:ALH79969.1, ECO:0000313|Proteomes:UP000058074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EY-1 {ECO:0000313|EMBL:ALH79969.1,
RC ECO:0000313|Proteomes:UP000058074};
RX PubMed=26634754;
RA Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA Tsuda M., Fujita N., Kawai F.;
RT "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP012700; ALH79969.1; -; Genomic_DNA.
DR RefSeq; WP_054587360.1; NZ_CP012700.1.
DR AlphaFoldDB; A0A0N9UY61; -.
DR KEGG; smag:AN936_06185; -.
DR PATRIC; fig|33050.5.peg.1290; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000058074; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR035671; DsbD_gamma.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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; PF11412; DsbD_N; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..637
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006039152"
FT TRANSMEM 294..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 380..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 493..510
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 498..637
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 637 AA; 66724 MW; 85AFB108491E0EF0 CRC64;
MERGQDGFVT RTWRGALALL ALAALAFTPA AARSTHITPK LVAESAAPAP GGTTTLALTM
VPEKTWHGYW SNGGDAGFGL QVEWNAPEGV TVEPFRYPVP DALILFGMMN HVYEHPYALL
ADVHIDKSIA PGTDLTLSGI ANWLACTDKV CVPEKAVISA ALKAGDGKVA ASDRERFDAW
RALLPQPLDR HGTWERRGDT LRFAIPLPAS TAIDAPHLFV ETRNLVDYAA PQNFSRNGDQ
IIVETRTKGE AGGPVTALLK LGSGRGLSLE LEPGTVPAAG EAIAGLSDEV DMGLFWTALG
GAIVGGLILN LMPCVFPILS LKALSLARSG GDARAAKVEA LAYTAGAALT ALLLGAILLG
LRAAGEQVGW AFQLQHPLSV FVLLLLAIAI TLNLAGVYEL PSFGGGQKLV EQGGAAGGFW
TGALAAFVAT PCSGPLLGAA LGATLVLPAW AALPIFGGLG FGIALPFLAI GFVPALRNRL
PKPGPWMARF RKWMAVPMAL TALALAVLLW RQIDGGWQDR GAQTAASANS FSPAALAKAR
ATGKPVFVYF TADWCLSCKA NEAGAINREA VQDVFKDKGV VTLVGDWTNG DPVITRTLAE
HGRNSVPLYL WYAPGAAKPE ILPQILTPGL LTDKAGG
//