ID A0A1R4H399_9GAMM Unreviewed; 647 AA.
AC A0A1R4H399;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:SJM90713.1};
GN ORFNames=CRENPOLYSF1_1530005 {ECO:0000313|EMBL:SJM90713.1};
OS Crenothrix polyspora.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Crenotrichaceae; Crenothrix.
OX NCBI_TaxID=360316 {ECO:0000313|EMBL:SJM90713.1, ECO:0000313|Proteomes:UP000195667};
RN [1] {ECO:0000313|EMBL:SJM90713.1, ECO:0000313|Proteomes:UP000195667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSM_CP1 {ECO:0000313|EMBL:SJM90713.1};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUKI01000061; SJM90713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4H399; -.
DR Proteomes; UP000195667; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036929; DsbDN_sf.
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; PF02683; DsbD; 1.
DR Pfam; PF13899; Thioredoxin_7; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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:UP000195667};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 195..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 377..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 439..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..495
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 503..647
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 647 AA; 70418 MW; CEC28E0B3A050D8F CRC64;
MRIDVMKNTL PIILLFLMSL LWVDIVFAEA PTAQVGVNVI NAKTWPTQYK ITLTIPKDHH
AYLDKGTENI YLPVAFDSEA KLANAGIKID KIEKPAGVYD AEVKATVLRE QGDFMLSLAQ
VGKAVTVANT AVDIDYQLCN DVTHVCFRPQ HTRAELPLPA LVAVVTKTVA PPVEQESLSF
TDKLLSLFKT NKDNAFIMFG LMLIAGLLSV ATPCVYPMLP ITSMFIVNRA NGKKDKEKHH
AGAYMVGMIG TYIVLGLLAG MTGGAFNTFM QSAAVNLAFA VFFAFFAVAL LGFYELSFMQ
NEVHTLDQKT TRVNGLGGTW MMGTVAGLVI SPCVGPIVFA LLLQVADNIA AKADALALVN
QSMGFWDKLL VASQGGFMMG GFGLGVALPF FIVSVVKFKK LPKAGYWMNK IKYAFGFMIL
YFAYIYFAKG MGVLGVDPAV TVSLAIGMVA IWIAVVHCHV LSLLPRDAMP NEKMHHYCGV
ITLLIGGWLM ASGMGNLPFI KTTQAGGALA SNSTQAVAMA GNERVAHEEA GITWYRSFAE
AQKVAQKTGK PIFIDFYASW CANCTAFKEE AASNESLNQA LREKAIAVKL IDKEPDFEKF
RIDPEHRPLK IGLPYFAILT PDGKVTWSGT DYKATEKMVS VLDGDAV
//
