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Database: UniProt
Entry: A6FC48_9GAMM
LinkDB: A6FC48_9GAMM
Original site: A6FC48_9GAMM 
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
//
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