ID U3A627_VIBPR Unreviewed; 394 AA.
AC U3A627;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000014};
GN Name=torC {ECO:0000313|EMBL:GAD69155.1};
GN ORFNames=VPR01S_24_00110 {ECO:0000313|EMBL:GAD69155.1};
OS Vibrio proteolyticus NBRC 13287.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1219065 {ECO:0000313|EMBL:GAD69155.1, ECO:0000313|Proteomes:UP000016570};
RN [1] {ECO:0000313|EMBL:GAD69155.1, ECO:0000313|Proteomes:UP000016570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13287 {ECO:0000313|EMBL:GAD69155.1,
RC ECO:0000313|Proteomes:UP000016570};
RA Isaki S., Hosoyama A., Numata M., Hashimoto M., Hosoyama Y., Tsuchikane K.,
RA Noguchi M., Hirakata S., Ichikawa N., Ohji S., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Vibrio proteolyticus NBRC 13287.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD69155.1}.
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DR EMBL; BATJ01000024; GAD69155.1; -; Genomic_DNA.
DR RefSeq; WP_021707123.1; NZ_BATJ01000024.1.
DR AlphaFoldDB; U3A627; -.
DR STRING; 1219065.VPR01S_24_00110; -.
DR eggNOG; COG3005; Bacteria.
DR Proteomes; UP000016570; Unassembled WGS sequence.
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:UP000016570};
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 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..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; 43832 MW; 7B9E8739643B3FD0 CRC64;
MKAFIVKFWH TLARPAIHIS LGVLTMGGFI AGVIFWGGFN TALEATNTEE FCISCHTMRD
NVYVELQETV HWKNHSGVRA TCPDCHVPHN WTDKIARKMQ ASKEVFAQVF GNYGEEGVFE
EHRIELAKHE WDRFSANKSL ECKNCHNYDS MDFEQMSPTA RIQMKQAAEK DQSCLDCHKG
IAHNLPKNMD SAAGIVGELE ALASNTDYAK GATLISVRHL PVYEDANATV EAGLLNPASA
VTVVDTKGEM VAVEISGWRK AKGFGRVIQE DFGMNIATAS LLKDAALSDA VVTKGEKRVD
ELTGLPWEQV TAKVWMKKQA MLNDITPVWE KAGAAYKTNC SVCHTQPKED HFDANTWPGM
FDGMLAFVNF DTDTEALVLK YLQKHSSDFS EGHH
//