ID Q6LPM7_PHOPR Unreviewed; 394 AA.
AC Q6LPM7;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000014};
GN Name=T3695 {ECO:0000313|EMBL:CAG20749.1};
GN OrderedLocusNames=PBPRA2364 {ECO:0000313|EMBL:CAG20749.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG20749.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004249}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004249}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- PTM: Binds 5 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000014-
CC 1}.
CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family.
CC {ECO:0000256|ARBA:ARBA00007395}.
CC -!- SIMILARITY: Belongs to the TorC/TorY family.
CC {ECO:0000256|ARBA:ARBA00006417, ECO:0000256|PIRNR:PIRNR000014}.
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DR EMBL; CR378670; CAG20749.1; -; Genomic_DNA.
DR RefSeq; WP_011219037.1; NC_006370.1.
DR AlphaFoldDB; Q6LPM7; -.
DR STRING; 298386.PBPRA2364; -.
DR KEGG; ppr:PBPRA2364; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_058814_0_0_6; -.
DR Proteomes; UP000000593; Chromosome 1.
DR GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3820.10; Di-heme elbow motif domain; 1.
DR InterPro; IPR009154; Membr-bd_4haem_cyt_TorC.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR InterPro; IPR038266; NapC/NirT_cytc_sf.
DR NCBIfam; TIGR02162; torC; 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; PIRSF000014; 4_hem_cytch_TorC; 1.
DR SUPFAM; SSF48695; Multiheme cytochromes; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|PIRNR:PIRNR000014};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR000014};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000014};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000014};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000014};
KW Membrane {ECO:0000256|PIRNR:PIRNR000014, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000014};
KW Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000014}.
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..187
FT /note="NapC/NirT cytochrome c N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03264"
FT BINDING 52
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 55
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 56
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:PIRSR000014-2"
FT BINDING 82
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 85
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 86
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:PIRSR000014-2"
FT BINDING 142
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 145
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 146
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:PIRSR000014-2"
FT BINDING 174
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 177
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 178
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:PIRSR000014-2"
FT BINDING 340
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 343
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-1"
FT BINDING 344
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="5"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR000014-2"
SQ SEQUENCE 394 AA; 44255 MW; 78AA70DA31778257 CRC64;
MMSFIKNLWG TFWRPAVHIS LGILTLGGFV AGVIFWGGFN TALEITNTEK FCIGCHEMKD
NVYEELQTTV HWSNNAGVRA TCPDCHVPHN WTDKIARKMQ ASKEVFGAIF GTIDTREKFL
AKRGELAQHE WKRFASNGSL ECKNCHQYES MKWEEMSPLA QSQMKQAAEK DQSCLDCHKG
IAHSLPDNMD TSGGMVSQLV SKSQNTSYTE GNNYFSVRYL PMYEDEALTQ SGGELNPASE
VKVVAVKGNA IQIEINGWRK TKGFGRVISE DFGMNIPTAA LSKDAAKNDT LVQKFEEKED
DLTGLPWQRV TVKLWMPKES LVDNVDMIWS ETKSAYTTNC SVCHTQPAEN HFDANTWPGM
FNGMLAFVNL DRDSEALVLK YLQKHSSDFS DSGH
//
