ID A0A0F7M4D3_9GAMM Unreviewed; 571 AA.
AC A0A0F7M4D3;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Thiol:disulfide interchange protein {ECO:0000313|EMBL:AKH69004.1};
DE EC=1.8.1.8 {ECO:0000313|EMBL:AKH69004.1};
GN ORFNames=IMCC21906_01326 {ECO:0000313|EMBL:AKH69004.1};
OS Spongiibacter sp. IMCC21906.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Spongiibacter.
OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH69004.1, ECO:0000313|Proteomes:UP000035013};
RN [1] {ECO:0000313|EMBL:AKH69004.1, ECO:0000313|Proteomes:UP000035013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH69004.1,
RC ECO:0000313|Proteomes:UP000035013};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21906 belonging to the
RT Gammaproteobacteria.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011477; AKH69004.1; -; Genomic_DNA.
DR RefSeq; WP_047011491.1; NZ_CP011477.1.
DR AlphaFoldDB; A0A0F7M4D3; -.
DR STRING; 1620392.IMCC21906_01326; -.
DR KEGG; spoi:IMCC21906_01326; -.
DR PATRIC; fig|1620392.3.peg.1388; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000035013; 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 CDD; cd02953; DsbDgamma; 1.
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; IPR035671; DsbD_gamma.
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; SSF74863; Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha); 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:AKH69004.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035013};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..571
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002518659"
FT TRANSMEM 187..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..402
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..151
FT /note="Thiol:disulfide interchange protein DsbD N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11412"
FT DOMAIN 195..370
FT /note="Cytochrome C biogenesis protein transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02683"
SQ SEQUENCE 571 AA; 62135 MW; 0891C7381CC9F952 CRC64;
MKSVLFVIML LISAYPSWAQ DPFAQSGSAP SEQMATADSA GFLPVNQAYQ SLLSWDDDTL
LLQWTITSGY YLYKERFAIS AELNGDALSP SIRFEPGKIK DDPYFGRTEV FYYNTSLSIS
GLPKDQPFVL TVRSQGCADA GLCYPPQIQR YQYKPQSHEF VQADATGSTA TAPAKVISTE
QNSAPSLAWV ITFAILGGAI LNLMPCVFPV LSLKVLSFSQ AEDGKTSSHG VIYSLGVIIS
FIVVAAVLIG LQQAGQAVGW GFQLQQPGFV AVMASLFFVL SLNLLGYFEI AGRWMNTGSS
LSQERGHSGS FFTGVLATLV ASPCTAPFMG TAVGYAATQP PAIALLVFAS LGAGMALPVL
LLSLFPGWLE ALPKPGAWME RLRQLLAFPL LASAIWLLWV YGRQLGANSM ATLLIAWLLI
AFALWLWKLG SKGKILSIIS LLLAVYTAMA GNHLPNNSQN SGQFDPAQIE KIRAAGSNVF
LDVTADWCIT CKANEKLVLH TPEIEQAFKD NNVHYLVADW TRYDPAITTL LAQYERNGIP
LYIYYSADPK QAVQILPQIL SKSLVLKLFE S
//
