CY553_DESVH
ID CY553_DESVH Reviewed; 103 AA.
AC P04032;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Cytochrome c-553;
DE AltName: Full=Cytochrome c553;
DE AltName: Full=Low-potential cytochrome c;
DE Flags: Precursor;
GN Name=cyf; OrderedLocusNames=DVU_1817;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2542232; DOI=10.1128/jb.171.6.3575-3578.1989;
RA van Rooijen G.J.H., Bruschi M., Voordouw G.;
RT "Cloning and sequencing of the gene encoding cytochrome c553 from
RT Desulfovibrio vulgaris Hildenborough.";
RL J. Bacteriol. 171:3575-3578(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8269917; DOI=10.1111/j.1432-1033.1993.tb18377.x;
RA Blanchard L., Marion D., Pollock B., Voordouw G., Wall J., Bruschi M.,
RA Guerlesquin F.;
RT "Overexpression of Desulfovibrio vulgaris Hildenborough cytochrome c553 in
RT Desulfovibrio desulfuricans G200. Evidence of conformational heterogeneity
RT in the oxidized protein by NMR.";
RL Eur. J. Biochem. 218:293-301(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
RN [4]
RP PROTEIN SEQUENCE OF 25-103.
RX PubMed=5038698; DOI=10.1016/0005-2795(72)90131-6;
RA Bruschi M., le Gall J.;
RT "C-type cytochromes of Desulfovibrio vulgaris. The primary structure of
RT cytochrome c 553.";
RL Biochim. Biophys. Acta 271:48-60(1972).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=1326323; DOI=10.1021/bi00150a008;
RA Marion D., Guerlesquin F.;
RT "Sequential NMR resonance assignment and secondary structure of
RT ferrocytochrome c553 from Desulfovibrio vulgaris Hildenborough.";
RL Biochemistry 31:8171-8179(1992).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=7844834; DOI=10.1006/jmbi.1994.0054;
RA Blackledge M.J., Medvedeva S., Poncin M., Guerlesquin F., Bruschi M.,
RA Marion D.;
RT "Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris
RT studied by NMR spectroscopy and restrained molecular dynamics.";
RL J. Mol. Biol. 245:661-681(1995).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=8766830; DOI=10.1016/0014-5793(96)00580-7;
RA Blanchard L., Blackledge M.J., Marion D., Guerlesquin F.;
RT "Investigation of oxidation state-dependent conformational changes in
RT Desulfovibrio vulgaris Hildenborough cytochrome c553 by two-dimensional H-
RT NMR spectra.";
RL FEBS Lett. 389:203-209(1996).
RN [8]
RP STRUCTURE BY NMR OF MUTANTS OF TYR-88.
RX PubMed=9490053; DOI=10.1046/j.1432-1327.1998.2510787.x;
RA Sebban-Kreuzer C., Blanchard L., Bersch B., Blackledge M.J., Marion D.,
RA Dolla A., Guerlesquin F.;
RT "1H-NMR study of the structural influence of Y64 substitution in
RT Desulfovibrio vulgaris Hildenborough cytochrome c553.";
RL Eur. J. Biochem. 251:787-794(1998).
RN [9]
RP STRUCTURE BY NMR OF MUTANT OF TYR-88.
RX PubMed=9622485; DOI=10.1021/bi980142u;
RA Sebban-Kreuzer C., Blackledge M., Dolla A., Marion D., Guerlesquin F.;
RT "Tyrosine 64 of cytochrome c553 is required for electron exchange with
RT formate dehydrogenase in Desulfovibrio vulgaris Hildenborough.";
RL Biochemistry 37:8331-8340(1998).
RN [10]
RP STRUCTURE BY NMR OF MUTANTS OF LYS-63 AND LYS-64.
RX PubMed=9654061; DOI=10.1046/j.1432-1327.1998.2530645.x;
RA Sebban-Kreuzer C., Dolla A., Guerlesquin F.;
RT "The formate dehydrogenase-cytochrome c553 complex from Desulfovibrio
RT vulgaris Hildenborough.";
RL Eur. J. Biochem. 253:645-652(1998).
CC -!- FUNCTION: Natural electron acceptor for a formate dehydrogenase.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is about +10 mV.;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 1 heme c group covalently per subunit.
CC -!- SEQUENCE CAUTION:
CC Sequence=Ref.4; Type=Miscellaneous discrepancy; Note=A number of tryptic peptides were mixed up.; Evidence={ECO:0000305};
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DR EMBL; M27062; AAA23356.1; -; Genomic_DNA.
DR EMBL; L25251; AAA16453.1; -; Unassigned_DNA.
DR EMBL; AE017285; AAS96294.1; -; Genomic_DNA.
DR PIR; A44752; A44752.
DR RefSeq; WP_010939104.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_011035.1; NC_002937.3.
DR PDB; 1DVH; NMR; -; A=25-103.
DR PDB; 1DWL; NMR; -; B=25-103.
DR PDB; 1E08; NMR; -; E=26-103.
DR PDB; 2DVH; NMR; -; A=25-103.
DR PDBsum; 1DVH; -.
DR PDBsum; 1DWL; -.
DR PDBsum; 1E08; -.
DR PDBsum; 2DVH; -.
DR AlphaFoldDB; P04032; -.
DR BMRB; P04032; -.
DR SMR; P04032; -.
DR STRING; 882.DVU_1817; -.
DR PaxDb; P04032; -.
DR EnsemblBacteria; AAS96294; AAS96294; DVU_1817.
DR KEGG; dvu:DVU_1817; -.
DR PATRIC; fig|882.5.peg.1667; -.
DR eggNOG; COG2863; Bacteria.
DR HOGENOM; CLU_128253_3_1_7; -.
DR OMA; MSMAMKA; -.
DR PhylomeDB; P04032; -.
DR EvolutionaryTrace; P04032; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; -; 1.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR PROSITE; PS51007; 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..24
FT /evidence="ECO:0000269|PubMed:5038698"
FT CHAIN 25..103
FT /note="Cytochrome c-553"
FT /evidence="ECO:0000269|PubMed:5038698"
FT /id="PRO_0000006535"
FT BINDING 34
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 37
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 38
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 81
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT CONFLICT 39
FT /note="G -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="S -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="K -> GK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:1DVH"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1DVH"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1DVH"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:2DVH"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:1DVH"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:1DVH"
FT HELIX 78..85
FT /evidence="ECO:0007829|PDB:1DVH"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:1DVH"
SQ SEQUENCE 103 AA; 10692 MW; 0AD6AA6408505DA4 CRC64;
MKRVLLLSSL CAALSFGLAV SGVAADGAAL YKSCIGCHGA DGSKAAMGSA KPVKGQGAEE
LYKKMKGYAD GSYGGERKAM MTNAVKKYSD EELKALADYM SKL
