YFCC_ALLVD
ID YFCC_ALLVD Reviewed; 184 AA.
AC Q06536; D3RRY0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative tetraheme cytochrome-c type;
DE AltName: Full=ORF1;
GN OrderedLocusNames=Alvin_1095;
OS Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS 10441 / D) (Chromatium vinosum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Allochromatium.
OX NCBI_TaxID=572477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX PubMed=22675582; DOI=10.4056/sigs.2335270;
RA Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL Stand. Genomic Sci. 5:311-330(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-184.
RX PubMed=8390993; DOI=10.1016/s0021-9258(19)85257-2;
RA Dolata M.M., van Beeumen J.J., Ambler R.P., Meyer T.E., Cusanovich M.A.;
RT "Nucleotide sequence of the heme subunit of flavocytochrome c from the
RT purple phototrophic bacterium, Chromatium vinosum. A 2.6-kilobase pair DNA
RT fragment contains two multiheme cytochromes, a flavoprotein, and a homolog
RT of human ankyrin.";
RL J. Biol. Chem. 268:14426-14431(1993).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- PTM: Binds 4 heme groups per subunit. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family. {ECO:0000305}.
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DR EMBL; CP001896; ADC62034.1; -; Genomic_DNA.
DR EMBL; L13419; AAA23314.1; -; Genomic_DNA.
DR PIR; A47169; A47169.
DR RefSeq; WP_012970310.1; NC_013851.1.
DR AlphaFoldDB; Q06536; -.
DR STRING; 572477.Alvin_1095; -.
DR EnsemblBacteria; ADC62034; ADC62034; Alvin_1095.
DR KEGG; alv:Alvin_1095; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_096753_2_0_6; -.
DR OMA; FCTGCHE; -.
DR OrthoDB; 1683334at2; -.
DR Proteomes; UP000001441; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 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 Pfam; PF03264; Cytochrom_NNT; 1.
DR PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..184
FT /note="Putative tetraheme cytochrome-c type"
FT /id="PRO_0000108440"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..184
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT BINDING 44
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 47
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 50
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:0000250|UniProtKB:Q72EF4"
FT BINDING 73
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 76
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 77
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:0000250|UniProtKB:Q72EF4"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 95
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:0000250|UniProtKB:Q72EF4"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 133
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 136
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 137
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:0000250|UniProtKB:Q72EF4"
FT BINDING 165
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 168
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 169
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:0000250|UniProtKB:Q72EF4"
FT BINDING 174
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:0000250|UniProtKB:Q72EF4"
FT CONFLICT 149
FT /note="Missing (in Ref. 2; AAA23314)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 20617 MW; 9472C54299DD0BED CRC64;
MSKHAASSAK RFSLLALGLM FVGGIVFVWA VDFGIKTTNT LEFCTSCHTM QTNFEEYKES
LHYKNTSGVQ ATCADCHVPK ELGPKLVTKI VAAKDVYHEV MGTIDTPEKF EARRWYLANL
VWKRLEASDS RECRSCHDYA DMDLSEQSRS ARSRHSAAQD KGQTCIECHK GVAHHEPTEP
DDAS
