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Database: UniProt
Entry: A0A078LKK4_9PSED
LinkDB: A0A078LKK4_9PSED
Original site: A0A078LKK4_9PSED 
ID   A0A078LKK4_9PSED        Unreviewed;       198 AA.
AC   A0A078LKK4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000013};
GN   Name=napC {ECO:0000313|EMBL:CDZ93228.1};
GN   ORFNames=BN1079_00515 {ECO:0000313|EMBL:CDZ93228.1};
OS   Pseudomonas saudiphocaensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1499686 {ECO:0000313|EMBL:CDZ93228.1, ECO:0000313|Proteomes:UP000053902};
RN   [1] {ECO:0000313|EMBL:CDZ93228.1, ECO:0000313|Proteomes:UP000053902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20_BN {ECO:0000313|EMBL:CDZ93228.1,
RC   ECO:0000313|Proteomes:UP000053902};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUL-2014) 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; CCSF01000001; CDZ93228.1; -; Genomic_DNA.
DR   RefSeq; WP_037022092.1; NZ_JADDOO010000002.1.
DR   AlphaFoldDB; A0A078LKK4; -.
DR   STRING; 1499686.BN1079_00515; -.
DR   eggNOG; COG3005; Bacteria.
DR   HOGENOM; CLU_096753_2_0_6; -.
DR   OrthoDB; 9782159at2; -.
DR   Proteomes; UP000053902; Unassembled WGS sequence.
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: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, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053902};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000013}.
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          18..192
FT                   /note="NapC/NirT cytochrome c N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03264"
FT   BINDING         55
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         58
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         61
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         85
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         88
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         89
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         107
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         145
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         148
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         149
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         178
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         181
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         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:0000256|PIRSR:PIRSR000013-2"
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:0000256|PIRSR:PIRSR000013-2"
SQ   SEQUENCE   198 AA;  22731 MW;  F1A3EA6D1FAFE85E CRC64;
     MKSLLAFLKR YWNVLSRPSV HYSLGALTLG GFIAGIIFWG GFNTALEATN TETFCISCHE
     MEDNVYMEIK ETIHYSNRSG VRATCPDCHV PHEWTDKIAR KMQASKEVWG KIFGTINTRE
     KFLGLRREMA EREWRRLKTN DSLECRNCHN FEYMDFTRQA PRAAQFHSTA LASGEATCID
     CHKGIAHRLP DMHGVPGW
//
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