CCMG_PARDP
ID CCMG_PARDP Reviewed; 179 AA.
AC P52236; A1B1W7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Thiol:disulfide interchange protein DsbE homolog;
DE AltName: Full=Cytochrome c biogenesis protein CcmG;
DE Flags: Precursor;
GN Name=ccmG; OrderedLocusNames=Pden_1410;
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=318586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9220005; DOI=10.1046/j.1365-2958.1997.4061775.x;
RA Page M.D., Ferguson S.J.;
RT "Paracoccus denitrificans CcmG is a periplasmic protein-disulphide
RT oxidoreductase required for c- and aa3-type cytochrome biogenesis; evidence
RT for a reductase role in vivo.";
RL Mol. Microbiol. 24:977-990(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some periplasmic
CC proteins. Also acts as a disulfide oxidoreductase in cytochromes c
CC biogenesis. The cysteines of apocytochromes c must be in the reduced
CC state for covalent linkage between the two moieties to occur.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the thioredoxin family. DsbE subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABL69511.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Z71971; CAA96497.1; -; Genomic_DNA.
DR EMBL; CP000489; ABL69511.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P52236; -.
DR SMR; P52236; -.
DR STRING; 318586.Pden_1410; -.
DR PRIDE; P52236; -.
DR EnsemblBacteria; ABL69511; ABL69511; Pden_1410.
DR KEGG; pde:Pden_1410; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_19_0_5; -.
DR Proteomes; UP000000361; Chromosome 1.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:UniProtKB-KW.
DR CDD; cd03010; TlpA_like_DsbE; 1.
DR InterPro; IPR004799; Periplasmic_diS_OxRdtase_DsbE.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF08534; Redoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR00385; dsbE; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Cytochrome c-type biogenesis; Disulfide bond; Periplasm;
KW Redox-active center; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..179
FT /note="Thiol:disulfide interchange protein DsbE homolog"
FT /id="PRO_0000034285"
FT DOMAIN 37..174
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 77..80
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT CONFLICT 28..29
FT /note="RD -> PN (in Ref. 1; CAA96497)"
FT /evidence="ECO:0000305"
FT CONFLICT 61..62
FT /note="ML -> IV (in Ref. 1; CAA96497)"
FT /evidence="ECO:0000305"
FT CONFLICT 145..146
FT /note="ID -> MH (in Ref. 1; CAA96497)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 19361 MW; DC802F6D5ADFA400 CRC64;
MARFSPMMLL PVAIFAGFAG LSGWALLRDD PDALPSAMIG REAPSVGEAT LPGKVQLTDE
MLRQPGVKLV NFWASWCPPC RAEHPTLTEL SARLPVYGVD LKDPEGAALG FLSEHGDPFH
ALAADPRGRV AIDWGVTAPP ETFIIDGSGR ILHRHAGPLV REDYTNRFLP ELEKALAAE