ID Q21MK3_SACD2 Unreviewed; 597 AA.
AC Q21MK3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=C-type cytochrome biogenesis protein {ECO:0000313|EMBL:ABD80076.1};
GN OrderedLocusNames=Sde_0814 {ECO:0000313|EMBL:ABD80076.1};
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122 {ECO:0000313|EMBL:ABD80076.1, ECO:0000313|Proteomes:UP000001947};
RN [1] {ECO:0000313|EMBL:ABD80076.1, ECO:0000313|Proteomes:UP000001947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 / ATCC 43961 / DSM 17024
RC {ECO:0000313|Proteomes:UP000001947};
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000282; ABD80076.1; -; Genomic_DNA.
DR RefSeq; WP_011467297.1; NC_007912.1.
DR AlphaFoldDB; Q21MK3; -.
DR STRING; 203122.Sde_0814; -.
DR KEGG; sde:Sde_0814; -.
DR eggNOG; COG4232; Bacteria.
DR HOGENOM; CLU_014657_0_1_6; -.
DR OrthoDB; 9811036at2; -.
DR Proteomes; UP000001947; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 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; 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.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001947};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004200240"
FT TRANSMEM 199..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..477
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 467..597
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 597 AA; 65490 MW; BEDFA7977F3B2066 CRC64;
MNIMTLKLLY RYVCAIFVSV LLLSAASTQA QGFLSSVDDG FLKVYDAYQV QPQTRQTDTT
TALNLEWKAA DGYYLYQHQF KAVARNATEG YKLALQIEPG IMKYDEYLEK ELEVFYNRAF
MQAEFPNLAP PYELMITSQG CADAGLCYPP YKHYFMVEAD GTILPMEAAS FSDATLTTLT
LPESAEATLA PKHAEAAPFL PLVMLSAILG GLILNLMPCV FPVLSLKALS FASSHVTPHK
QHAHGWAYTL GAVLSFVGFA VIMLVAREAG EQLGWGFQLT NPVFVAFMVY LFFFMGLVLS
GFVELGGGWM GMGQNLTSGE GIKSSFFTGV LAAVVASPCS GPFMATALGI AITQHAAIAI
IIFACLGFGM ALPFLLLSYN PKLTNRLPAP GVWMDTLKQF FAFPLYLTGV WLLWVLGHQV
NSDAAAALVM GAVLIAFSFW LFKQTTQSKT WNVIRLATAI ASLVIALGIA IAAKWFAAPT
QYEWEPYSAR DLAAYRKEGT PVFVDLTADW CTTCKVNEFV ALNTEEVQNK AEELGIVMMQ
GDWTNGEEAI TQYLEQFGRN SVPLYLMYPA TPDTPPVVLP QFLSKSLVLE AMQKAVP
//
