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Database: UniProt
Entry: K0JK17_BRAPL
LinkDB: K0JK17_BRAPL
Original site: K0JK17_BRAPL 
ID   K0JK17_BRAPL            Unreviewed;       569 AA.
AC   K0JK17;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Thiol disulfide interchange protein {ECO:0000313|EMBL:CCG56650.1};
GN   Name=dsbD {ECO:0000313|EMBL:CCG56650.1};
GN   ORFNames=WESB_1181 {ECO:0000313|EMBL:CCG56650.1};
OS   Brachyspira pilosicoli WesB.
OC   Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC   Brachyspira.
OX   NCBI_TaxID=1161918 {ECO:0000313|EMBL:CCG56650.1, ECO:0000313|Proteomes:UP000003759};
RN   [1] {ECO:0000313|EMBL:CCG56650.1, ECO:0000313|Proteomes:UP000003759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WesB {ECO:0000313|EMBL:CCG56650.1};
RX   PubMed=22947175; DOI=10.1186/1471-2164-13-454;
RA   Mappley L.J., Black M.L., Abuoun M., Darby A.C., Woodward M.J.,
RA   Parkhill J., Turner A.K., Bellgard M.I., La T., Phillips N.D.,
RA   La Ragione R.M., Hampson D.J.;
RT   "Comparative genomics of Brachyspira pilosicoli strains: genome
RT   rearrangements, reductions and correlation of genetic compliment with
RT   phenotypic diversity.";
RL   BMC Genomics 13:454-454(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; HE793032; CCG56650.1; -; Genomic_DNA.
DR   RefSeq; WP_014932983.1; NC_018604.1.
DR   AlphaFoldDB; K0JK17; -.
DR   KEGG; bpw:WESB_1181; -.
DR   PATRIC; fig|1161918.5.peg.485; -.
DR   HOGENOM; CLU_015841_0_0_12; -.
DR   OrthoDB; 7629852at2; -.
DR   Proteomes; UP000003759; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        165..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        299..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        368..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        397..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          430..568
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   569 AA;  63942 MW;  1A75F2C91ED8F4E7 CRC64;
     MRKIYIFLFI IFSLTAYSQS FNSLLNKNTE AIIVFSLSTN DNKITVKANI PEGYYAYLES
     KIANKILFFA DNKEINTTYP EGEKYHEDII IKGEQEFILN DIDINKINFI KTTYQLCSAK
     DNVCLQPKSK VIYGEEIDIP NNNITDEKPE NASSIENYIK GSNNIFITLI LIFAAGLASV
     LLPCTYPLLS ITVSILGTTT DEKNNKKSSV LASLLFALGV ITTYTLLGAV VSVAGFAFHK
     TILFGSIGYN PIVLTILVLL FLYFTFSMAG FYEIKAPSFL QSAKTNAYAK KNQSIFHKYI
     MGLLAGIVAT PCAAPIIAVI LEIGFLNPVF ATLYMAVYAL GFASVLFILG TFASILTKMP
     KAGTWMVYVK YIFTFLMMII SFYYANILFG VLGFNKISYI LASVTILVFA LLVYIIKNKT
     AMLSSLEKKI FVSVLIISIV LGSIYGIIKQ KSEVSNLVTY NEALELSKQN NKPILIDFSA
     VWCANCYELK EKVFVNEELK KFIDDNLIFT EVDVDKYKNI SDEYNVKWLP WIIVIDSDKN
     ILYTKNSFSS FDDKMALSIK EDLEKVINK
//
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