CY552_ACIFI
ID CY552_ACIFI Reviewed; 230 AA.
AC P74917;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cytochrome c-552;
DE AltName: Full=Cytochrome c552;
DE Flags: Precursor;
GN Name=cyc1;
OS Acidithiobacillus ferridurans.
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1232575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RA Appia C., Bengrine A., Chippaux M., Cavazza C., Bruschi M., Bonnefoy V.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 48-95, MASS SPECTROMETRY, AND CHARACTERIZATION.
RX PubMed=8973648; DOI=10.1111/j.1432-1033.1996.0308r.x;
RA Cavazza C., Giudici-Orticoni M.-T., Nitschke W., Appia C., Bonnefoy V.,
RA Bruschi M.;
RT "Characterisation of a soluble cytochrome c4 isolated from Thiobacillus
RT ferrooxidans.";
RL Eur. J. Biochem. 242:308-314(1996).
CC -!- FUNCTION: Diheme, high potential cytochrome c.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) are +385 +/- 20 mV and +480 +/- 20 mV.;
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Binds 2 heme c groups covalently per subunit.
CC -!- MASS SPECTROMETRY: Mass=21193; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8973648};
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DR EMBL; AJ006456; CAA07032.1; -; Genomic_DNA.
DR PDB; 1H1O; X-ray; 2.13 A; A/B=48-230.
DR PDBsum; 1H1O; -.
DR AlphaFoldDB; P74917; -.
DR SMR; P74917; -.
DR STRING; 380394.Lferr_2750; -.
DR BioCyc; MetaCyc:MON-16160; -.
DR EvolutionaryTrace; P74917; -.
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:0005506; F:iron ion binding; IEA:InterPro.
DR Gene3D; 1.10.760.10; -; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR024167; Cytochrome_c4-like.
DR Pfam; PF00034; Cytochrom_C; 2.
DR PIRSF; PIRSF000005; Cytochrome_c4; 1.
DR SUPFAM; SSF46626; SSF46626; 2.
DR PROSITE; PS51007; CYTC; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Electron transport; Heme; Iron;
KW Metal-binding; Periplasm; Signal; Transport.
FT SIGNAL 1..47
FT /evidence="ECO:0000269|PubMed:8973648"
FT CHAIN 48..230
FT /note="Cytochrome c-552"
FT /id="PRO_0000006534"
FT BINDING 63
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 66
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 67
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 166
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 169
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 170
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT CONFLICT 89
FT /note="Y -> YI (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 105..110
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:1H1O"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:1H1O"
FT HELIX 217..229
FT /evidence="ECO:0007829|PDB:1H1O"
SQ SEQUENCE 230 AA; 25298 MW; D7622872E7B1AF57 CRC64;
MTTYLSQDRL RNKENDTMTY QHSKMYQSRT FLLFSALLLV AGQASAAVGS ADAPAPYRVS
SDCMVCHGMT GRDTLYPIVP RLAGQHKSYM EAQLKAYKDH SRADQNGEIY MWPVAQALDS
AKITALADYF NAQKPPMQSS GIKHAGAKEG KAIFNQGVTN EQIPACMECH GSDGQGAGPF
PRLAGQRYGY IIQQLTYFHN GTRVNTLMNQ IAKNITVAQM KDVAAYLSSL
