CYC3_SHEFN
ID CYC3_SHEFN Reviewed; 111 AA.
AC O33731; Q084G0;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Tetraheme cytochrome c-type;
DE AltName: Full=Cytochrome c3;
DE Flags: Precursor;
GN Name=cctA; OrderedLocusNames=Sfri_1504;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-51,
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RX PubMed=10861223; DOI=10.1042/0264-6021:3490153;
RA Gordon E.H.J., Pike A.D., Hill A.E., Cuthbertson P.M., Chapman S.K.,
RA Reid G.A.;
RT "Identification and characterization of a novel cytochrome c3 from
RT Shewanella frigidimarina that is involved in Fe(III) respiration.";
RL Biochem. J. 349:153-158(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP STRUCTURE BY NMR OF THE HEME CORE.
RX PubMed=11231004; DOI=10.1016/s0014-5793(00)02383-8;
RA Pessanha M., Brennan L., Xavier A.V., Cuthbertson P.M., Reid G.A.,
RA Chapman S.K., Turner D.L., Salgueiro C.A.;
RT "NMR structure of the haem core of a novel tetrahaem cytochrome isolated
RT from Shewanella frigidimarina: identification of the haem-specific axial
RT ligands and order of oxidation.";
RL FEBS Lett. 489:8-13(2001).
CC -!- FUNCTION: Transfers electrons to ferredoxin III.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 4 heme groups per subunit.
CC -!- MASS SPECTROMETRY: Mass=11778; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10861223, ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ000006; CAA03850.1; -; Genomic_DNA.
DR EMBL; CP000447; ABI71355.1; -; Genomic_DNA.
DR RefSeq; WP_011636975.1; NC_008345.1.
DR PDB; 2K3V; NMR; -; A=26-111.
DR PDBsum; 2K3V; -.
DR AlphaFoldDB; O33731; -.
DR BMRB; O33731; -.
DR SMR; O33731; -.
DR STRING; 318167.Sfri_1504; -.
DR EnsemblBacteria; ABI71355; ABI71355; Sfri_1504.
DR KEGG; sfr:Sfri_1504; -.
DR eggNOG; COG1053; Bacteria.
DR HOGENOM; CLU_164073_0_0_6; -.
DR OMA; YEFEQCQ; -.
DR OrthoDB; 738283at2; -.
DR EvolutionaryTrace; O33731; -.
DR Proteomes; UP000000684; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR012286; Tetrahaem_cytochrome.
DR Pfam; PF14537; Cytochrom_c3_2; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:10861223"
FT CHAIN 26..111
FT /note="Tetraheme cytochrome c-type"
FT /id="PRO_0000006506"
FT BINDING 34
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 BINDING 40
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 43
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 44
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 BINDING 60
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 63
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT BINDING 64
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 BINDING 74
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 BINDING 77
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 BINDING 83
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 86
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT BINDING 87
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 BINDING 90
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 BINDING 100
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 103
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT BINDING 104
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 HELIX 30..35
FT /evidence="ECO:0007829|PDB:2K3V"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:2K3V"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:2K3V"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2K3V"
FT HELIX 54..59
FT /evidence="ECO:0007829|PDB:2K3V"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:2K3V"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:2K3V"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:2K3V"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2K3V"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2K3V"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:2K3V"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:2K3V"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:2K3V"
SQ SEQUENCE 111 AA; 11882 MW; 9902BF1878812A73 CRC64;
MSNKLLSALF AAGFAVMMMS SASFAADETL AEFHVEMGGC ENCHADGEPS KDGAYEFEQC
QSCHGSLAEM DDNHKPHDGL LMCADCHAPH EAKVGEKPTC DTCHDDGRTA K
