NAPC_ECOLI
ID NAPC_ECOLI Reviewed; 200 AA.
AC P0ABL5; P33932; Q2MAP1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cytochrome c-type protein NapC;
GN Name=napC; Synonyms=yejX; OrderedLocusNames=b2202, JW2190;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CHARACTERIZATION AS A CYTOCHROME C.
RX PubMed=8039676; DOI=10.1111/j.1574-6968.1994.tb06872.x;
RA Iobbi-Nivol C., Crooke H., Griffiths L., Grov J., Hussain H., Pommier J.,
RA Mejean V., Cole J.A.;
RT "A reassessment of the range of c-type cytochromes synthesized by
RT Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 119:89-94(1994).
CC -!- FUNCTION: Mediates electron flow from quinones to the NapAB complex.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC protein.
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; U00008; AAA16394.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75262.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76665.1; -; Genomic_DNA.
DR PIR; H64989; H64989.
DR RefSeq; NP_416706.1; NC_000913.3.
DR RefSeq; WP_000528376.1; NZ_SSZK01000027.1.
DR AlphaFoldDB; P0ABL5; -.
DR BioGRID; 4261930; 10.
DR DIP; DIP-10306N; -.
DR IntAct; P0ABL5; 43.
DR STRING; 511145.b2202; -.
DR TCDB; 3.D.11.1.1; the periplasmic nitrate reductase complex (nap) complex family.
DR jPOST; P0ABL5; -.
DR PaxDb; P0ABL5; -.
DR PRIDE; P0ABL5; -.
DR EnsemblBacteria; AAC75262; AAC75262; b2202.
DR EnsemblBacteria; BAE76665; BAE76665; BAE76665.
DR GeneID; 66673903; -.
DR GeneID; 946706; -.
DR KEGG; ecj:JW2190; -.
DR KEGG; eco:b2202; -.
DR PATRIC; fig|1411691.4.peg.34; -.
DR EchoBASE; EB1990; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_096753_2_0_6; -.
DR InParanoid; P0ABL5; -.
DR OMA; FCTGCHE; -.
DR PhylomeDB; P0ABL5; -.
DR BioCyc; EcoCyc:NAPC-MON; -.
DR PRO; PR:P0ABL5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IMP:EcoCyc.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..200
FT /note="Cytochrome c-type protein NapC"
FT /id="PRO_0000108432"
FT TOPO_DOM 1..23
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 45..200
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
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 /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 63
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 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 90
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 91
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 103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 109
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 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 150
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 151
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 179
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 /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 183
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 188
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"
SQ SEQUENCE 200 AA; 23101 MW; E86A62ABE46AAAA3 CRC64;
MGNSDRKPGL IKRLWKWWRT PSRLALGTLL LIGFVGGIVF WGGFNTGMEK ANTEEFCISC
HEMRNTVYQE YMDSVHYNNR SGVRATCPDC HVPHEFVPKM IRKLKASKEL YGKIFGVIDT
PQKFEAHRLT MAQNEWRRMK DNNSQECRNC HNFEYMDTTA QKSVAAKMHD QAVKDGQTCI
DCHKGIAHKL PDMREVEPGF
