ID   NAPC_ECOL6              Reviewed;         200 AA.
AC   P0ABL6; P33932;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Cytochrome c-type protein NapC;
GN   Name=napC; OrderedLocusNames=c2739;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
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DR   EMBL; AE014075; AAN81193.1; -; Genomic_DNA.
DR   RefSeq; WP_000528376.1; NZ_CP051263.1.
DR   AlphaFoldDB; P0ABL6; -.
DR   STRING; 199310.c2739; -.
DR   GeneID; 75206454; -.
DR   KEGG; ecc:c2739; -.
DR   eggNOG; COG3005; Bacteria.
DR   HOGENOM; CLU_096753_2_0_6; -.
DR   BioCyc; ECOL199310:C2739-MONOMER; -.
DR   Proteomes; UP000001410; Chromosome.
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; Di-heme elbow motif domain; 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   NCBIfam; TIGR02161; napC_nirT; 1.
DR   PANTHER; PTHR30333; CYTOCHROME C-TYPE PROTEIN; 1.
DR   PANTHER; PTHR30333:SF1; CYTOCHROME C-TYPE PROTEIN NAPC; 1.
DR   Pfam; PF03264; Cytochrom_NNT; 1.
DR   PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1.
DR   SUPFAM; SSF48695; Multiheme cytochromes; 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_0000108434"
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
//