ID F9YSH0_CAPCC Unreviewed; 677 AA.
AC F9YSH0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Protein-disulfide reductase {ECO:0000313|EMBL:AEK22643.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:AEK22643.1};
GN OrderedLocusNames=Ccan_05230 {ECO:0000313|EMBL:AEK22643.1};
OS Capnocytophaga canimorsus (strain 5).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=860228 {ECO:0000313|EMBL:AEK22643.1, ECO:0000313|Proteomes:UP000008895};
RN [1] {ECO:0000313|EMBL:AEK22643.1, ECO:0000313|Proteomes:UP000008895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5 {ECO:0000313|Proteomes:UP000008895};
RX PubMed=21914877; DOI=10.1128/JB.05853-11;
RA Manfredi P., Pagni M., Cornelis G.R.;
RT "Complete genome sequence of the dog commensal and human pathogen
RT Capnocytophaga canimorsus strain 5.";
RL J. Bacteriol. 193:5558-5559(2011).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002113; AEK22643.1; -; Genomic_DNA.
DR RefSeq; WP_013996635.1; NC_015846.1.
DR AlphaFoldDB; F9YSH0; -.
DR STRING; 860228.Ccan_05230; -.
DR KEGG; ccm:Ccan_05230; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_015841_0_0_10; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000008895; Chromosome.
DR GO; GO:0016020; C: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 Gene3D; 2.60.40.1250; Thiol:disulfide interchange protein DsbD, N-terminal domain; 1.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR028250; DsbDN.
DR InterPro; IPR036929; DsbDN_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AEK22643.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008895};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..677
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003395808"
FT TRANSMEM 200..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 392..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..446
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 467..485
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..139
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 209..397
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
FT REGION 166..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 74916 MW; 2B966631BD3A79D0 CRC64;
MKKLLSIIFT LFVVFSNAQI HDPVSWQTKV EKTAENEFSL IVTAQIERGW RLYAQNIPPN
GPVPTTFEFE KSPDYQLVGK VSEEKVMTKF DNVFNMEIGY FSEKAVFTQK IKTSQPIKNI
KGTVEFMVCD DSTCLPPDTI DLVFAFDEFF AGSQNAQNDL AQITGDTSQN TSSEAHKQTD
KKTIETPSVS ESNSDLAKKG LWAIFFISFL SGFAALLTPC VFPMIPMTVS YFTKQSKSKA
QGIKNAVFYG VSIIVIYVLL GTGVTAIFGA DALNALASNV WFNLIFFILL VFFAASFLGA
FELTLPSSWS TKVDAQANRS GLVGIFFMAL ALAIVSFSCT GPIVGTLLVE AASRGGIAPI
IGMFGFSLAI ALPFALFAAF PGWLNSLPKS GGWLNTVKVV LGFLELALAF KFLSQADLVL
QLHFLEREVF IAIWIAVFGT LALYLFGKIR LPHDSPIQHI SVGRLSLGLL SLTFTIYMIP
GLWGAPLNLI SAFPPPQHYS ESPYGVGYTK MGGGVSAINE ANLPEGASLL EPNNILHFVD
YQQGLDYAKK VNKPVLIDFT GWACVNCRKM EQNVWPKPQI LEILKNEVVF ISLYVDDKRP
LPAEQVTESK VRPGRKIKYI GQKWSEFQTL RYKANSQPFY VLMNHDESNL ITPIGYTPDA
DEFLQWLKAG VGNFNKK
//
