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Database: UniProt
Entry: B0VJM7_CLOAI
LinkDB: B0VJM7_CLOAI
Original site: B0VJM7_CLOAI 
ID   B0VJM7_CLOAI            Unreviewed;       612 AA.
AC   B0VJM7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Putative thiol:disulfide interchange protein dsbD (DsbD-like) (Protein-disulfide reductase) (Disulfide reductase) putative membrane protein {ECO:0000313|EMBL:CAO81712.1};
DE            EC=1.8.1.8 {ECO:0000313|EMBL:CAO81712.1};
GN   OrderedLocusNames=CLOAM1885 {ECO:0000313|EMBL:CAO81712.1};
OS   Cloacimonas acidaminovorans (strain Evry).
OC   Bacteria; Candidatus Cloacimonadota; Candidatus Cloacimonadia;
OC   Candidatus Cloacimonadales; Candidatus Cloacimonadaceae; Cloacimonas.
OX   NCBI_TaxID=459349 {ECO:0000313|EMBL:CAO81712.1, ECO:0000313|Proteomes:UP000002019};
RN   [1] {ECO:0000313|EMBL:CAO81712.1, ECO:0000313|Proteomes:UP000002019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Evry {ECO:0000313|Proteomes:UP000002019};
RX   PubMed=18245282; DOI=10.1128/JB.01248-07;
RA   Pelletier E., Kreimeyer A., Bocs S., Rouy Z., Gyapay G., Chouari R.,
RA   Riviere D., Ganesan A., Daegelen P., Sghir A., Cohen G.N., Medigue C.,
RA   Weissenbach J., Le Paslier D.;
RT   "'Candidatus Cloacamonas acidaminovorans': genome sequence reconstruction
RT   provides a first glimpse of a new bacterial division.";
RL   J. Bacteriol. 190:2572-2579(2008).
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DR   EMBL; CU466930; CAO81712.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0VJM7; -.
DR   STRING; 459349.CLOAM1885; -.
DR   KEGG; caci:CLOAM1885; -.
DR   eggNOG; COG4232; Bacteria.
DR   HOGENOM; CLU_014657_1_0_0; -.
DR   Proteomes; UP000002019; 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   InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR   InterPro; IPR028250; DsbDN.
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:CAO81712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002019};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        199..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..263
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        354..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        421..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        452..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          69..142
FT                   /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11412"
FT   DOMAIN          203..405
FT                   /note="Cytochrome C biogenesis protein transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02683"
SQ   SEQUENCE   612 AA;  68173 MW;  BC6FF5C5542E92A2 CRC64;
     MLMHRCLKLL LMFCLVLLIL PIFAQSVKFS ISPEVLKPGE KGVIKATLLI PEGKKQTFNP
     QNPEYFYLEA SHPDLILGKV IYPKPTQVVS EEEWNYHPQV TLTLPFTVKQ TAKTGNKQIE
     VLLSYNLCYE TGMCDPPEEA TAILSIKIAE NEPIPAAVSE NEEETPNRIE QKETIPIEKS
     PIPDKKPETS HPLGEILKYI LFAFLGGIIL NITPCVLPIL PIRIMSIMNQ AQKDKTKVLN
     HTLIYALGVL ISFAVMAGIF IALQKAGESV GWGLQNQNPG FVVTLMSIVF VFALSLLGVF
     EITVPGMNTA NKATSRGGYS GSFFGGIFAF LMAISCTGPF LGAALPFALA LPPVLMLIFF
     LTIGLGFAFP FLLIGFFPKA LKIIPKPGNW MIIFKEVMGF VLLIIVYTQL KTLLLLTDGE
     YLLKVLWFLF ILGFSTWLYG RFVRVENSKL TQWLFTLISI GLIIFAAVTY LPIKETKQEE
     IQVKSGELIP APNAPEGWYV FSEDILNKAL KEGRAVFLDI GAAWCKNCMT NEKTVLFTET
     MMQEFKKKNV LLLRGDFTKK DETLLAWIKK HGRAGVPFNA LYIPGAEPHI FGELLSKDEV
     INALNKIPAQ AE
//
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