NAPC_ECO57
ID NAPC_ECO57 Reviewed; 200 AA.
AC P0ABL7; P33932;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cytochrome c-type protein NapC;
GN Name=napC; OrderedLocusNames=Z3459, ECs3091;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Mediates electron flow from quinones to the NapAB complex.
CC {ECO:0000250}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG57337.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36514.1; -; Genomic_DNA.
DR PIR; C91015; C91015.
DR PIR; E85859; E85859.
DR RefSeq; NP_311118.1; NC_002695.1.
DR RefSeq; WP_000528376.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ABL7; -.
DR STRING; 155864.EDL933_3367; -.
DR EnsemblBacteria; AAG57337; AAG57337; Z3459.
DR EnsemblBacteria; BAB36514; BAB36514; ECs_3091.
DR GeneID; 66673903; -.
DR GeneID; 916797; -.
DR KEGG; ece:Z3459; -.
DR KEGG; ecs:ECs_3091; -.
DR PATRIC; fig|386585.9.peg.3225; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_096753_2_0_6; -.
DR OMA; FCTGCHE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IEA:UniProt.
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 3: Inferred from homology;
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_0000108433"
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
