ID   C553_PARDE              Reviewed;         226 AA.
AC   P29967;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cytochrome c-553I;
DE   AltName: Full=Cytochrome c553I;
DE   Flags: Precursor;
GN   Name=cycB;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Pd 1235;
RX   PubMed=1657873; DOI=10.1128/jb.173.21.6971-6979.1991;
RA   Ras J., Reijnders W.N.M., van Spanning R.J.M., Harms N., Oltmann L.F.,
RA   Stouthamer A.H.;
RT   "Isolation, sequencing, and mutagenesis of the gene encoding cytochrome
RT   c553i of Paracoccus denitrificans and characterization of the mutant
RT   strain.";
RL   J. Bacteriol. 173:6971-6979(1991).
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: During growth on methanol.
CC   -!- PTM: Binds 1 heme group per subunit.
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DR   EMBL; M75583; AAA25575.1; -; Genomic_DNA.
DR   PIR; B41378; B41378.
DR   AlphaFoldDB; P29967; -.
DR   SMR; P29967; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015945; P:methanol metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR022411; C-typ_cyt_methanol_metab-rel.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   TIGRFAMs; TIGR03874; 4cys_cytochr; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Methanol utilization; Periplasm; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..226
FT                   /note="Cytochrome c-553I"
FT                   /id="PRO_0000006539"
FT   REGION          43..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         125
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   226 AA;  23879 MW;  C1D5DAB03702AEC7 CRC64;
     MTSKTTASLL AICVACAASA IAGTALCADR RNAPAQAGAG AAAAVSGDAH EQPAAEAPAE
     EEEETPAVAA TDGKLVLPNG QDITPDHMEN GRWYTAEDIP TYKIAEEGAV DWATFSGYRR
     YSAECHVCHG PDGEGSTYAP ALRKSVLTMG YYDFLEIAAS GKQEVNTAAN LVMPAFGTNK
     NVWCYIDDIY AYLLARGTGD LPRGRPAKRE DKSDEFVAQE DSCMSG