AURB_CHLAA
ID AURB_CHLAA Reviewed; 235 AA.
AC P27197; A9WE06; P94610;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Auracyanin-B;
DE Short=Ac-B;
DE Contains:
DE RecName: Full=Auracyanin-B-1;
DE Contains:
DE RecName: Full=Auracyanin-B-2;
DE Flags: Precursor;
GN OrderedLocusNames=Caur_1950;
OS Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=324602;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lopez J.C., Dracheva S., Blankenship R.E.;
RT "Gene sequence for auracyanin B from Chloroflexus aurantiacus.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT "Complete genome sequence of the filamentous anoxygenic phototrophic
RT bacterium Chloroflexus aurantiacus.";
RL BMC Genomics 12:334-334(2011).
RN [3]
RP PROTEIN SEQUENCE OF 81-235, FUNCTION, COPPER BINDING, SUBCELLULAR LOCATION,
RP AND GLYCOSYLATION.
RX PubMed=1313011; DOI=10.1016/s0021-9258(19)50460-4;
RA McManus J.D., Brune D.C., Han J., Sanders-Loehr J., Meyer T.E.,
RA Cusanovich M.A., Tollin G., Blankenship R.E.;
RT "Isolation, characterization, and amino acid sequences of auracyanins, blue
RT copper proteins from the green photosynthetic bacterium Chloroflexus
RT aurantiacus.";
RL J. Biol. Chem. 267:6531-6540(1992).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12589566; DOI=10.1007/s00775-002-0416-5;
RA Rooney M.B., Honeychurch M.J., Selvaraj F.M., Blankenship R.E., Bond A.M.,
RA Freeman H.C.;
RT "A thin-film electrochemical study of the 'blue' copper proteins,
RT auracyanin A and auracyanin B, from the photosynthetic bacterium
RT Chloroflexus aurantiacus: the reduction potential as a function of pH.";
RL J. Biol. Inorg. Chem. 8:306-317(2003).
RN [5]
RP INDUCTION.
RC STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX PubMed=19190939; DOI=10.1007/s00775-009-0473-0;
RA Lee M., del Rosario M.C., Harris H.H., Blankenship R.E., Guss J.M.,
RA Freeman H.C.;
RT "The crystal structure of auracyanin A at 1.85 A resolution: the structures
RT and functions of auracyanins A and B, two almost identical 'blue' copper
RT proteins, in the photosynthetic bacterium Chloroflexus aurantiacus.";
RL J. Biol. Inorg. Chem. 14:329-345(2009).
RN [6]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22249883; DOI=10.1007/s11120-011-9711-8;
RA Cao L., Bryant D.A., Schepmoes A.A., Vogl K., Smith R.D., Lipton M.S.,
RA Callister S.J.;
RT "Comparison of Chloroflexus aurantiacus strain J-10-fl proteomes of cells
RT grown chemoheterotrophically and photoheterotrophically.";
RL Photosyn. Res. 110:153-168(2012).
RN [7]
RP REVIEW.
RX PubMed=23357331; DOI=10.1016/j.bbabio.2013.01.008;
RA Majumder E.L., King J.D., Blankenship R.E.;
RT "Alternative Complex III from phototrophic bacteria and its electron
RT acceptor auracyanin.";
RL Biochim. Biophys. Acta 1827:1383-1391(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 81-235.
RX PubMed=11178893; DOI=10.1006/jmbi.2000.4201;
RA Bond C.S., Blankenship R.E., Freeman H.C., Guss J.M., Maher M.J.,
RA Selvaraj F.M., Wilce M.C.J., Willingham K.M.;
RT "Crystal structure of auracyanin, a 'blue' copper protein from the green
RT thermophilic photosynthetic bacterium Chloroflexus aurantiacus.";
RL J. Mol. Biol. 306:47-67(2001).
CC -!- FUNCTION: Probably a soluble electron acceptor for the integral
CC membrane protein electron transfer alternative complex III (ACIII).
CC {ECO:0000269|PubMed:1313011}.
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 +190 mV at pH 9, +215 mV at pH 7 and +240 mV at pH 4.
CC {ECO:0000269|PubMed:12589566};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:1313011};
CC Peripheral membrane protein {ECO:0000305|PubMed:1313011}. Note=Possibly
CC located on the extracellular face of the cell membrane.
CC -!- INDUCTION: Present in both photosynthetically (anaerobically) and dark
CC (aerobic respiration) grown cells (at protein level) (PubMed:19190939).
CC A later paper showed this protein to be present in both
CC chemoheterotrophically (dark) and photoheterotrophically (light) grown
CC cells, but with more protein present in light grown cells
CC (PubMed:22249883). The second report is thought to be correct
CC (PubMed:23357331). {ECO:0000269|PubMed:19190939,
CC ECO:0000269|PubMed:22249883, ECO:0000269|PubMed:23357331}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:1313011}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; U78046; AAB38318.1; -; Genomic_DNA.
DR EMBL; CP000909; ABY35165.1; -; Genomic_DNA.
DR RefSeq; WP_012257819.1; NC_010175.1.
DR RefSeq; YP_001635554.1; NC_010175.1.
DR PDB; 1OV8; X-ray; 1.90 A; A/B/C/D=96-235.
DR PDB; 1QHQ; X-ray; 1.55 A; A=96-235.
DR PDBsum; 1OV8; -.
DR PDBsum; 1QHQ; -.
DR AlphaFoldDB; P27197; -.
DR SMR; P27197; -.
DR STRING; 324602.Caur_1950; -.
DR EnsemblBacteria; ABY35165; ABY35165; Caur_1950.
DR KEGG; cau:Caur_1950; -.
DR PATRIC; fig|324602.8.peg.2219; -.
DR eggNOG; COG3241; Bacteria.
DR HOGENOM; CLU_102862_0_0_0; -.
DR InParanoid; P27197; -.
DR OMA; HNWVLVN; -.
DR EvolutionaryTrace; P27197; -.
DR Proteomes; UP000002008; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0009767; P:photosynthetic electron transport chain; IDA:UniProtKB.
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 Pfam; PF00127; Copper-bind; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS00196; COPPER_BLUE; 1.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Direct protein sequencing;
KW Electron transport; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Signal; Transport.
FT SIGNAL 1..56
FT /evidence="ECO:0000255"
FT PROPEP 57..80
FT /evidence="ECO:0000269|PubMed:1313011"
FT /id="PRO_0000002846"
FT CHAIN 81..235
FT /note="Auracyanin-B-1"
FT /id="PRO_0000002847"
FT CHAIN 89..235
FT /note="Auracyanin-B-2"
FT /id="PRO_0000002848"
FT DOMAIN 111..235
FT /note="Plastocyanin-like"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 222
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 227
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT CONFLICT 183
FT /note="P -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="P -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="F -> G (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..226
FT /note="YLAG -> TPI (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:1QHQ"
FT HELIX 161..172
FT /evidence="ECO:0007829|PDB:1QHQ"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:1QHQ"
FT TURN 220..226
FT /evidence="ECO:0007829|PDB:1QHQ"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:1QHQ"
SQ SEQUENCE 235 AA; 23716 MW; 845186230C072521 CRC64;
MSWRGSGRSN FRSRSSSNGG STFSGGSAGG PPLIVMMGLA FGAGLIMLIV MIASNATAGG
FVAATPRPTA TPRPTAAPAP TQPPAAQPTT APATQAANAP GGSNVVNETP AQTVEVRAAP
DALAFAQTSL SLPANTVVRL DFVNQNNLGV QHNWVLVNGG DDVAAAVNTA AQNNADALFV
PPPDTPNALA WTAMLNAGES GSVTFRTPAP GTYLYICTFP GHYLAGMKGT LTVTP
