ID   NORC_PARDE              Reviewed;         150 AA.
AC   Q51662;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Nitric oxide reductase subunit C;
DE   AltName: Full=NOR small subunit;
DE   AltName: Full=Nitric oxide reductase cytochrome c subunit;
GN   Name=norC;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Pd 1222;
RX   PubMed=9022686; DOI=10.1111/j.1432-1033.1996.0592r.x;
RA   de Boer A.P.N., van der Oost J., Reijnders W.N.M., Westerhoff H.V.,
RA   Stouthamer A.H., van Spanning R.J.;
RT   "Mutational analysis of the nor gene cluster which encodes nitric-oxide
RT   reductase from Paracoccus denitrificans.";
RL   Eur. J. Biochem. 242:592-600(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NBRC 12442;
RA   Murai K., Miyake K., Andoh J., Iijima S.;
RT   "Cloning and nucleotide sequence of the nitric oxide reductase locus in
RT   Paracoccus denitrificans IFO 12442.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   EPR SPECTROSCOPY.
RX   PubMed=9748316; DOI=10.1021/bi980943x;
RA   Hendriks J., Warne A., Gohlke U., Haltia T., Ludovici C., Luebben M.,
RA   Saraste M.;
RT   "The active site of the bacterial nitric oxide reductase is a dinuclear
RT   iron center.";
RL   Biochemistry 37:13102-13109(1998).
CC   -!- FUNCTION: Component of the anaerobic respiratory chain that transforms
CC       nitrate to dinitrogen (denitrification).
CC   -!- SUBUNIT: Heterodimer of cytochromes b (large subunit) and c (small
CC       subunit).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass membrane
CC       protein {ECO:0000250}. Note=May be attached to the membrane by a
CC       signal-anchor. {ECO:0000250}.
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DR   EMBL; U28078; AAA68970.1; -; Genomic_DNA.
DR   EMBL; AB014090; BAA32545.1; -; Genomic_DNA.
DR   RefSeq; WP_011748764.1; NZ_PPGA01000003.1.
DR   AlphaFoldDB; Q51662; -.
DR   SMR; Q51662; -.
DR   TCDB; 3.D.4.10.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR   PRIDE; Q51662; -.
DR   OMA; WPPNIEG; -.
DR   BioCyc; MetaCyc:MON-16873; -.
DR   BRENDA; 1.7.2.5; 3341.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
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:0016966; F:nitric oxide reductase activity; IMP:CACAO.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Respiratory chain; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..150
FT                   /note="Nitric oxide reductase subunit C"
FT                   /id="PRO_0000108422"
FT   TRANSMEM        13..29
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         65
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         66
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   150 AA;  16992 MW;  779645910F471258 CRC64;
     MSEIMTKNMA RNVFYGGSIF FILIFGALTV HSHIYARTKA VDESQLTPSV VEGKHIWERN
     ACIDCHTLLG EGAYFAPELG NVMKRWGVQD DPDSAFETLK GWMESMPTGI EGRRQMPRFD
     LTDEEFRALS DFLLWTGTIN TQNWPPNDAG