ID A0A127JZV9_9BURK Unreviewed; 696 AA.
AC A0A127JZV9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:AMO25403.1};
GN ORFNames=UC35_12010 {ECO:0000313|EMBL:AMO25403.1};
OS Ramlibacter tataouinensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=94132 {ECO:0000313|EMBL:AMO25403.1, ECO:0000313|Proteomes:UP000070433};
RN [1] {ECO:0000313|EMBL:AMO25403.1, ECO:0000313|Proteomes:UP000070433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-10 {ECO:0000313|EMBL:AMO25403.1,
RC ECO:0000313|Proteomes:UP000070433};
RX PubMed=24425747; DOI=10.1099/ijs.0.058396-0;
RA Lee H.J., Lee S.H., Lee S.S., Lee J.S., Kim Y., Kim S.C., Jeon C.O.;
RT "Ramlibacter solisilvae sp. nov., isolated from forest soil, and emended
RT description of the genus Ramlibacter.";
RL Int. J. Syst. Evol. Microbiol. 64:1317-1322(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP010951; AMO25403.1; -; Genomic_DNA.
DR RefSeq; WP_061503809.1; NZ_CP010951.1.
DR AlphaFoldDB; A0A127JZV9; -.
DR PATRIC; fig|94132.3.peg.2444; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000070433; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd02953; DsbDgamma; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR035671; DsbD_gamma.
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; 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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000070433};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 298..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 426..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..518
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 524..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 550..571
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 574..696
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 696 AA; 73850 MW; 9749E1932D30AF62 CRC64;
MVALLPLLAA AQGGAKSVVT TDRVRAELLA HAPDGIAPGR QVWLGLQLAH KPEWHTYWKN
SGDSGLPTQL TWTLPRGVEA GEIAWPVPRK IPIGALANYG YEGTVLLPVP LTITPEFKAP
LAGDLEVRLK ANWLVCKKEC IPEEGDFVLK VPARSTTALN AAQFQQAFDA QPRPLDGGGS
TARIEGSALA ITVQGLPATL RGKPLEFFPE TGEVVETGAQ WTQAWKGEAW TAQVPLSPQR
AASPTAMPVV LASNGQGWRT ELKVVGAWPA AQAAPAGLPP SLEAALRENA RAPATPSIGF
AAALLGALLG GLILNLMPCV FPILAIKVVG FTRHADDHRG HRISGLAYTA GVVVSFAGLA
ALMLALRAAG EQLGWGFQLQ SPAVVAVLAA LFTIIGLNLA GVFEFRSFLP SRWATMQAKH
PVADAFLTGV LAVAVASPCT APFMGASLGL AIALPAAEAL AIFAVLGLGM ALPYLVASWV
PPVARWLPRP GAWMETFRRL MAFPMFGTVV WLVWVLGQQS GIDGAGALLA LLVALSMTVW
ALTLRGRVRL ALGALALASF GLLAWTAGGA ITRVATAQPA GAQERWQAWA PGRVDQLLAE
GRPVFVDFTA AWCVTCQYNK KTTLTDREVL ADFESRNFAL LRADWTRRDP AITEALAQLG
RSGVPVYVVY RQGRPPVVLS EVIGVEEVRS VINNEL
//
