ID Q8D0X5_YERPE Unreviewed; 205 AA.
AC Q8D0X5; Q74SF3;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 118.
DE RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000013};
GN Name=napC {ECO:0000313|EMBL:AAM85018.1};
GN OrderedLocusNames=y1447 {ECO:0000313|EMBL:AAM85018.1}, YP_2659
GN {ECO:0000313|EMBL:AAS62851.1};
OS Yersinia pestis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632 {ECO:0000313|EMBL:AAM85018.1, ECO:0000313|Proteomes:UP000002490};
RN [1] {ECO:0000313|EMBL:AAM85018.1, ECO:0000313|Proteomes:UP000002490}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM {ECO:0000313|EMBL:AAM85018.1}, and KIM10+ / Biovar
RC Mediaevalis {ECO:0000313|Proteomes:UP000002490};
RX PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G.III., Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plana G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2] {ECO:0000313|EMBL:AAS62851.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=91001 {ECO:0000313|EMBL:AAS62851.1};
RA Song Y., Tong Z., Wang L., Han Y., Zhang J., Pei D., Wang J., Zhou D.,
RA Han Y., Pang X., Zhai J., Chen F., Qin H., Wang J., Li S., Guo Z., Ye C.,
RA Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000001019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis {ECO:0000313|Proteomes:UP000001019};
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [4] {ECO:0000313|EMBL:AAS62851.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=91001 {ECO:0000313|EMBL:AAS62851.1};
RA Yiqing M.;
RT "Reannotation of Yersinia pestis strain 91001 based on omics data.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000013-1};
CC Note=Binds 4 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000013-
CC 1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000256|PIRNR:PIRNR000013}.
CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family.
CC {ECO:0000256|ARBA:ARBA00007395}.
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DR EMBL; AE009952; AAM85018.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62851.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8D0X5; -.
DR DNASU; 1146394; -.
DR EnsemblBacteria; AAS62851; AAS62851; YP_2659.
DR KEGG; ypk:y1447; -.
DR KEGG; ypm:YP_2659; -.
DR HOGENOM; CLU_096753_2_0_6; -.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000013};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000013};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000013};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000013};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000013}.
FT DOMAIN 27..198
FT /note="NapC/NirT cytochrome c N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03264"
FT BINDING 62
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 65
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 68
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:0000256|PIRSR:PIRSR000013-2"
FT BINDING 92
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 95
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 96
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:0000256|PIRSR:PIRSR000013-2"
FT BINDING 114
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:0000256|PIRSR:PIRSR000013-2"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 155
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 156
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:0000256|PIRSR:PIRSR000013-2"
FT BINDING 184
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 187
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT BINDING 188
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:0000256|PIRSR:PIRSR000013-2"
FT BINDING 193
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:0000256|PIRSR:PIRSR000013-2"
SQ SEQUENCE 205 AA; 23459 MW; 7134071A8AFDDA80 CRC64;
MISEGMMSET KKPGFIRRLW QWWRRPSRLA LGTLLLIGFV SGIIFWGGFN TGMEMANTEK
FCISCHEMKD NVYEEYMSTI HYSNRSGVKA TCPDCHVPHE WGPKMVRKIK ASKELYAKAF
GLIDTPQKFD AHRLTMAESE WARMKANDSQ ECRNCHNFDN MDFSAQKTVA AKMHSQAITE
GKTCIDCHKG IAHKLPDMKD VPIGF
//
