ID A6FC48_9GAMM Unreviewed; 190 AA.
AC A6FC48;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000013};
GN ORFNames=PE36_12537 {ECO:0000313|EMBL:EDM67272.1};
OS Moritella sp. PE36.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=58051 {ECO:0000313|EMBL:EDM67272.1, ECO:0000313|Proteomes:UP000004278};
RN [1] {ECO:0000313|EMBL:EDM67272.1, ECO:0000313|Proteomes:UP000004278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PE36 {ECO:0000313|EMBL:EDM67272.1,
RC ECO:0000313|Proteomes:UP000004278};
RA Yayanos A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JUN-2007) 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 -!- 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}.
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:EDM67272.1}.
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DR EMBL; ABCQ01000014; EDM67272.1; -; Genomic_DNA.
DR RefSeq; WP_006031960.1; NZ_ABCQ01000014.1.
DR AlphaFoldDB; A6FC48; -.
DR STRING; 58051.PE36_12537; -.
DR OrthoDB; 9782159at2; -.
DR Proteomes; UP000004278; 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 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 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 17..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..184
FT /note="NapC/NirT cytochrome c N-terminal"
FT /evidence="ECO:0000259|Pfam:PF03264"
FT BINDING 50
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 53
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 77
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 80
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 81
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 99
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 137
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 140
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 141
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 170
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 173
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 174
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 179
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 190 AA; 21590 MW; AD10071C95D8D54A CRC64;
MKLILNFWRK LTTPSKAAVG TVLAMGFLGG IIFWGAFNMG MEATNTEEFC SACHAPIVKE
LRETIHYSNR SGVRAICSDC HVPHNWTDKI VRKVQASNEI VAFLMGTIST QEKFEARRKH
LAVREWQRMK ENDSQECRNC HNFEYMDFSE QGPRSRKQHS TALASGEKTC VDCHKGIAHQ
LPDMSDVPGW
//