NAPC_CERS4
ID NAPC_CERS4 Reviewed; 227 AA.
AC Q53178; Q3IV41;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cytochrome c-type protein NapC;
GN Name=napC; OrderedLocusNames=RHOS4_40250; ORFNames=RSP_4118;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OG Plasmid pRS241c.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8730872; DOI=10.1111/j.1365-2958.1996.tb02475.x;
RA Reyes F., Roldan M.D., Klipp W., Castillo F., Moreno-Vivian C.;
RT "Isolation of periplasmic nitrate reductase genes from Rhodobacter
RT sphaeroides DSM 158: structural and functional differences among
RT prokaryotic nitrate reductases.";
RL Mol. Microbiol. 19:1307-1318(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.; PLASMID=pRS241c;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of plasmid C of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Mediates electron flow from quinones to the NapAB complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC protein.
CC -!- INDUCTION: Nitrate reductase activity can be induced by nitrate and not
CC repressed by ammonium or oxygen.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family. {ECO:0000305}.
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DR EMBL; Z46806; CAA86828.1; -; Genomic_DNA.
DR EMBL; CP000146; ABA81593.1; -; Genomic_DNA.
DR RefSeq; WP_011331400.1; NZ_CP030275.1.
DR RefSeq; YP_345334.1; NC_007489.1.
DR AlphaFoldDB; Q53178; -.
DR DNASU; 3711834; -.
DR EnsemblBacteria; ABA81593; ABA81593; RSP_4118.
DR KEGG; rsp:RSP_4118; -.
DR PATRIC; fig|272943.9.peg.180; -.
DR OMA; FCTGCHE; -.
DR PhylomeDB; Q53178; -.
DR Proteomes; UP000002703; Plasmid pRS241c.
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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019333; P:denitrification pathway; IEA:InterPro.
DR Gene3D; 1.10.3820.10; -; 1.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR024717; NapC/NirT/NrfH.
DR InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR InterPro; IPR038266; NapC/NirT_cytc_sf.
DR InterPro; IPR011885; NO3Rdtase_cyt_c_NapC/NirT.
DR Pfam; PF03264; Cytochrom_NNT; 1.
DR PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR TIGRFAMs; TIGR02161; napC_nirT; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Plasmid; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..227
FT /note="Cytochrome c-type protein NapC"
FT /id="PRO_0000108437"
FT TOPO_DOM 1..19
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..227
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 54
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 57
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 60
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 84
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 87
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 88
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 106
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 144
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 147
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 148
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 178
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 181
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 182
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 187
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT CONFLICT 81
FT /note="R -> S (in Ref. 1; CAA86828)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> T (in Ref. 1; CAA86828)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 227 AA; 25637 MW; 360664417C6F9DD9 CRC64;
MRLPSFLRRF WSIATSPSSF LSVGFLTLGG FVGGVLFWGG FNTALEATNT EAFCTSCHEM
QSNVFEELTR TVHYTNRSGV RAGCPDCHVP HEWTDKIARK MQASKEVWGH LFGTIDTRRK
FLDNRLRLAE HEWARLKAND SLECRNCHSE VAMDFTRQTD RAAQIHTQYL IQTEGYTCID
CHKGIAHELP DMRGIDPGWL PPADLRASLP DHGSSFDLEG ARAYVAD
