RUS2_ACIFI
ID RUS2_ACIFI Reviewed; 187 AA.
AC P0C918; P24930; P74919; Q56297; Q56298;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Rusticyanin;
DE Flags: Precursor;
GN Name=rus; Synonyms=rusTA;
OS Acidithiobacillus ferridurans.
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1232575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX PubMed=9838063; DOI=10.1016/s0167-4781(98)00199-7;
RA Bengrine A., Guiliani N., Appia-Ayme C., Jedlicki E., Holmes D.S.,
RA Chippaux M., Bonnefoy V.;
RT "Sequence and expression of the rusticyanin structural gene from
RT Thiobacillus ferrooxidans ATCC33020 strain.";
RL Biochim. Biophys. Acta 1443:99-112(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=8947572; DOI=10.1006/jmbi.1996.0612;
RA Walter R.L., Ealick S.E., Friedman A.M., Blake R.C. II, Proctor P.,
RA Shoham M.;
RT "Multiple wavelength anomalous diffraction (MAD) crystal structure of
RT rusticyanin: a highly oxidizing cupredoxin with extreme acid stability.";
RL J. Mol. Biol. 263:730-751(1996).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RA Zhao D., Shoham M.;
RL Submitted (JAN-1998) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=9761859; DOI=10.1107/s0907444998005423;
RA Harvey I., Hao Q., Duke E.M., Ingledew W.J., Hasnain S.S.;
RT "Structure determination of a 16.8 kDa copper protein at 2.1-A resolution
RT using anomalous scattering data with direct methods.";
RL Acta Crystallogr. D 54:629-635(1998).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=8947573; DOI=10.1006/jmbi.1996.0613;
RA Botuyan M.V., Toy-Palmer A., Chung J., Blake R.C. II, Beroza P., Case D.A.,
RA Dyson H.J.;
RT "NMR solution structure of Cu(I) rusticyanin from Thiobacillus
RT ferrooxidans: structural basis for the extreme acid stability and redox
RT potential.";
RL J. Mol. Biol. 263:752-767(1996).
CC -!- FUNCTION: Electron carrier from cytochrome c552 to the A-type oxidase.
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 1 copper ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Redox potential:
CC E(0) is +680 mV.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- INDUCTION: Expressed during growth on Fe(2+), sulfur and thiosulfate.
CC {ECO:0000269|PubMed:9838063}.
CC -!- CAUTION: The two different versions of rusticyanins are most probably
CC due to strain variations. {ECO:0000305}.
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DR EMBL; AJ006456; CAA07038.1; -; Genomic_DNA.
DR PDB; 1A3Z; X-ray; 1.90 A; A=33-187.
DR PDB; 1A8Z; X-ray; 2.10 A; A=39-187.
DR PDB; 1CUR; NMR; -; A=38-187.
DR PDB; 1E30; X-ray; 1.50 A; A/B=38-187.
DR PDB; 1GY1; X-ray; 1.65 A; A/B=38-187.
DR PDB; 1GY2; X-ray; 1.82 A; A/B=38-187.
DR PDB; 1RCY; X-ray; 1.90 A; A=38-187.
DR PDB; 2CAK; X-ray; 1.27 A; A=38-187.
DR PDB; 2CAL; X-ray; 1.10 A; A=38-187.
DR PDBsum; 1A3Z; -.
DR PDBsum; 1A8Z; -.
DR PDBsum; 1CUR; -.
DR PDBsum; 1E30; -.
DR PDBsum; 1GY1; -.
DR PDBsum; 1GY2; -.
DR PDBsum; 1RCY; -.
DR PDBsum; 2CAK; -.
DR PDBsum; 2CAL; -.
DR AlphaFoldDB; P0C918; -.
DR SMR; P0C918; -.
DR STRING; 380394.Lferr_2743; -.
DR BioCyc; MetaCyc:MON-16161; -.
DR EvolutionaryTrace; P0C918; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR CDD; cd04231; Rusticyanin; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR000923; BlueCu_1.
DR InterPro; IPR028871; BlueCu_1_BS.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR001243; Rusticyanin.
DR Pfam; PF00127; Copper-bind; 1.
DR PRINTS; PR00158; RUSTICYANIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR TIGRFAMs; TIGR03095; rusti_cyanin; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Electron transport; Metal-binding; Periplasm; Signal;
KW Transport.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..187
FT /note="Rusticyanin"
FT /id="PRO_0000002872"
FT DOMAIN 85..187
FT /note="Plastocyanin-like"
FT BINDING 117
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 170
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 180
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2CAL"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2CAL"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:2CAL"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:2CAL"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:2CAL"
SQ SEQUENCE 187 AA; 19857 MW; BA1DA44A5BE95981 CRC64;
MYTQNTMKKN WYVTVGAAAA LAATVGMGTA MAGTLDSTWK EATLPQVKAM LEKDTGKVSG
DTVTYSGKTV HVVAAAVLPG FPFPSFEVHD KKNPTLEIPA GATVDVTFIN TNKGFGHSFD
ITKKGPPYAV MPVIDPIVAG TGFSPVPKDG KFGYTDFTWH PTAGTYYYVC QIPGHAATGM
FGKIIVK
