NORC_PSEAE
ID NORC_PSEAE Reviewed; 146 AA.
AC Q59646;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 144.
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=PA0523;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=7711073; DOI=10.1016/0167-4781(95)00018-c;
RA Arai H., Igarashi Y., Kodama T.;
RT "The structural genes for nitric oxide reductase from Pseudomonas
RT aeruginosa.";
RL Biochim. Biophys. Acta 1261:279-284(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; Single-pass membrane protein.
CC Note=May be attached to the membrane by a signal-anchor.
CC -!- INDUCTION: By nitric oxide. {ECO:0000305}.
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DR EMBL; D38133; BAA07329.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03912.1; -; Genomic_DNA.
DR PIR; S53712; S53712.
DR RefSeq; NP_249214.1; NC_002516.2.
DR RefSeq; WP_003113238.1; NZ_QZGE01000010.1.
DR PDB; 3O0R; X-ray; 2.70 A; C=1-146.
DR PDB; 3WFB; X-ray; 2.70 A; C=1-146.
DR PDB; 3WFC; X-ray; 2.50 A; C=1-146.
DR PDB; 3WFD; X-ray; 2.30 A; C=1-146.
DR PDB; 3WFE; X-ray; 2.49 A; C=1-146.
DR PDB; 5GUW; X-ray; 3.20 A; A/C=1-146.
DR PDB; 5GUX; X-ray; 3.30 A; C=1-146.
DR PDBsum; 3O0R; -.
DR PDBsum; 3WFB; -.
DR PDBsum; 3WFC; -.
DR PDBsum; 3WFD; -.
DR PDBsum; 3WFE; -.
DR PDBsum; 5GUW; -.
DR PDBsum; 5GUX; -.
DR AlphaFoldDB; Q59646; -.
DR SMR; Q59646; -.
DR STRING; 287.DR97_3491; -.
DR TCDB; 3.D.4.10.3; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; Q59646; -.
DR PRIDE; Q59646; -.
DR ABCD; Q59646; 1 sequenced antibody.
DR DNASU; 882200; -.
DR EnsemblBacteria; AAG03912; AAG03912; PA0523.
DR GeneID; 882200; -.
DR KEGG; pae:PA0523; -.
DR PATRIC; fig|208964.12.peg.553; -.
DR PseudoCAP; PA0523; -.
DR HOGENOM; CLU_135564_0_0_6; -.
DR InParanoid; Q59646; -.
DR OMA; WPPNIEG; -.
DR PhylomeDB; Q59646; -.
DR BioCyc; PAER208964:G1FZ6-528-MON; -.
DR BRENDA; 1.7.2.5; 5087.
DR Proteomes; UP000002438; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Respiratory chain; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..146
FT /note="Nitric oxide reductase subunit C"
FT /id="PRO_0000108424"
FT TRANSMEM 13..29
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 64
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 /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT HELIX 7..39
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3WFD"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3O0R"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3WFD"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 87..100
FT /evidence="ECO:0007829|PDB:3WFD"
FT HELIX 119..132
FT /evidence="ECO:0007829|PDB:3WFD"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3WFD"
SQ SEQUENCE 146 AA; 16344 MW; 1C0DB7E59431CC98 CRC64;
MSETFTKGMA RNIYFGGSVF FILLFLALTY HTEKTLPERT NEAAMSAAVV RGKLVWEQNN
CVGCHTLLGE GAYFAPELGN VVGRRGGEEG FNTFLQAWMN IQPLNVPGRR AMPQFHLSEG
QVDDLAEFLK WSSKIDTNQW PPNKEG
