ID   NORC_CERS5              Reviewed;         147 AA.
AC   O06844; A4WR57;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 4.
DT   03-AUG-2022, entry version 124.
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; OrderedLocusNames=Rsph17025_0970;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9171397; DOI=10.1128/jb.179.11.3534-3540.1997;
RA   Bartnikas T.B., Tosques I.E., Laratta W.P., Shi J., Shapleigh J.P.;
RT   "Characterization of the nitric oxide reductase-encoding region in
RT   Rhodobacter sphaeroides 2.4.3.";
RL   J. Bacteriol. 179:3534-3540(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
RG   US DOE Joint Genome Institute;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
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; AF000233; AAC45371.1; -; Genomic_DNA.
DR   EMBL; CP000661; ABP69871.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06844; -.
DR   SMR; O06844; -.
DR   STRING; 349102.Rsph17025_0970; -.
DR   EnsemblBacteria; ABP69871; ABP69871; Rsph17025_0970.
DR   KEGG; rsq:Rsph17025_0970; -.
DR   eggNOG; COG2010; Bacteria.
DR   HOGENOM; CLU_135564_0_0_5; -.
DR   OMA; WPPNIEG; -.
DR   OrthoDB; 1469969at2; -.
DR   BioCyc; RSPH349102:G1G8M-995-MON; -.
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   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..147
FT                   /note="Nitric oxide reductase subunit C"
FT                   /id="PRO_0000108426"
FT   TRANSMEM        13..29
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   BINDING         59
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
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         63
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"
FT   CONFLICT        103..104
FT                   /note="QP -> HA (in Ref. 1; AAC45371)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16403 MW;  86BAC985ADBB0AFA CRC64;
     MSEILTKSRA RNVFYGGSLF FIAVFVGLTV QSHNYVVSTT PALTDEVILG KHVWERNSCI
     NCHTLHGEGA YFAPEVGNVM TRWGVLDDPD AAAEMLGGWM DAQPSGVEGR RQMPHFELTD
     EEKRGLSEFL RWADQMNTQS WPPNDAG