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Auracyanin-B (Ac-B) [Cleaved into: Auracyanin-B-1; Auracyanin-B-2]

 AURB_CHLAA              Reviewed;         235 AA.
P27197; A9WE06; P94610;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
28-FEB-2018, entry version 122.
RecName: Full=Auracyanin-B;
Short=Ac-B;
Contains:
RecName: Full=Auracyanin-B-1;
Contains:
RecName: Full=Auracyanin-B-2;
Flags: Precursor;
OrderedLocusNames=Caur_1950;
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
Chloroflexaceae; Chloroflexus.
NCBI_TaxID=324602;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lopez J.C., Dracheva S., Blankenship R.E.;
"Gene sequence for auracyanin B from Chloroflexus aurantiacus.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
PubMed=21714912; DOI=10.1186/1471-2164-12-334;
Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
"Complete genome sequence of the filamentous anoxygenic phototrophic
bacterium Chloroflexus aurantiacus.";
BMC Genomics 12:334-334(2011).
[3]
PROTEIN SEQUENCE OF 81-235, FUNCTION, COPPER BINDING, SUBCELLULAR
LOCATION, AND GLYCOSYLATION.
PubMed=1313011;
McManus J.D., Brune D.C., Han J., Sanders-Loehr J., Meyer T.E.,
Cusanovich M.A., Tollin G., Blankenship R.E.;
"Isolation, characterization, and amino acid sequences of auracyanins,
blue copper proteins from the green photosynthetic bacterium
Chloroflexus aurantiacus.";
J. Biol. Chem. 267:6531-6540(1992).
[4]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12589566; DOI=10.1007/s00775-002-0416-5;
Rooney M.B., Honeychurch M.J., Selvaraj F.M., Blankenship R.E.,
Bond A.M., Freeman H.C.;
"A thin-film electrochemical study of the 'blue' copper proteins,
auracyanin A and auracyanin B, from the photosynthetic bacterium
Chloroflexus aurantiacus: the reduction potential as a function of
pH.";
J. Biol. Inorg. Chem. 8:306-317(2003).
[5]
INDUCTION.
STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
PubMed=19190939; DOI=10.1007/s00775-009-0473-0;
Lee M., del Rosario M.C., Harris H.H., Blankenship R.E., Guss J.M.,
Freeman H.C.;
"The crystal structure of auracyanin A at 1.85 A resolution: the
structures and functions of auracyanins A and B, two almost identical
'blue' copper proteins, in the photosynthetic bacterium Chloroflexus
aurantiacus.";
J. Biol. Inorg. Chem. 14:329-345(2009).
[6]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22249883; DOI=10.1007/s11120-011-9711-8;
Cao L., Bryant D.A., Schepmoes A.A., Vogl K., Smith R.D., Lipton M.S.,
Callister S.J.;
"Comparison of Chloroflexus aurantiacus strain J-10-fl proteomes of
cells grown chemoheterotrophically and photoheterotrophically.";
Photosyn. Res. 110:153-168(2012).
[7]
REVIEW.
PubMed=23357331; DOI=10.1016/j.bbabio.2013.01.008;
Majumder E.L., King J.D., Blankenship R.E.;
"Alternative Complex III from phototrophic bacteria and its electron
acceptor auracyanin.";
Biochim. Biophys. Acta 1827:1383-1391(2013).
[8]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 81-235.
PubMed=11178893; DOI=10.1006/jmbi.2000.4201;
Bond C.S., Blankenship R.E., Freeman H.C., Guss J.M., Maher M.J.,
Selvaraj F.M., Wilce M.C.J., Willingham K.M.;
"Crystal structure of auracyanin, a 'blue' copper protein from the
green thermophilic photosynthetic bacterium Chloroflexus
aurantiacus.";
J. Mol. Biol. 306:47-67(2001).
-!- FUNCTION: Probably a soluble electron acceptor for the integral
membrane protein electron transfer alternative complex III
(ACIII). {ECO:0000269|PubMed:1313011}.
-!- COFACTOR:
Name=Cu cation; Xref=ChEBI:CHEBI:23378;
Note=Binds 1 copper ion per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Redox potential:
E(0) is +190 mV at pH 9, +215 mV at pH 7 and +240 mV at pH 4.
{ECO:0000269|PubMed:12589566};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:1313011};
Peripheral membrane protein {ECO:0000305|PubMed:1313011}.
Note=Possibly located on the extracellular face of the cell
membrane.
-!- INDUCTION: Present in both photosynthetically (anaerobically) and
dark (aerobic respiration) grown cells (at protein level)
(PubMed:19190939). A later paper showed this protein to be present
in both chemoheterotrophically (dark) and photoheterotrophically
(light) grown cells, but with more protein present in light grown
cells (PubMed:22249883). The second report is thought to be
correct (PubMed:23357331). {ECO:0000269|PubMed:19190939,
ECO:0000269|PubMed:22249883, ECO:0000269|PubMed:23357331}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:1313011}.
-!- SIMILARITY: Belongs to the multicopper oxidase family.
{ECO:0000305}.
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EMBL; U78046; AAB38318.1; -; Genomic_DNA.
EMBL; CP000909; ABY35165.1; -; Genomic_DNA.
RefSeq; WP_012257819.1; NC_010175.1.
RefSeq; YP_001635554.1; NC_010175.1.
PDB; 1OV8; X-ray; 1.90 A; A/B/C/D=96-235.
PDB; 1QHQ; X-ray; 1.55 A; A=96-235.
PDBsum; 1OV8; -.
PDBsum; 1QHQ; -.
ProteinModelPortal; P27197; -.
SMR; P27197; -.
STRING; 324602.Caur_1950; -.
EnsemblBacteria; ABY35165; ABY35165; Caur_1950.
GeneID; 5826401; -.
KEGG; cau:Caur_1950; -.
PATRIC; fig|324602.8.peg.2219; -.
eggNOG; ENOG4105UTB; Bacteria.
eggNOG; COG3241; LUCA.
HOGENOM; HOG000034233; -.
InParanoid; P27197; -.
OMA; HNWVLVN; -.
OrthoDB; POG091H0LOW; -.
BioCyc; CAUR324602:G1GAO-1977-MONOMER; -.
EvolutionaryTrace; P27197; -.
Proteomes; UP000002008; Chromosome.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0009767; P:photosynthetic electron transport chain; IDA:UniProtKB.
Gene3D; 2.60.40.420; -; 1.
InterPro; IPR000923; BlueCu_1.
InterPro; IPR028871; BlueCu_1_BS.
InterPro; IPR033138; Cu_oxidase_CS.
InterPro; IPR008972; Cupredoxin.
Pfam; PF00127; Copper-bind; 1.
SUPFAM; SSF49503; SSF49503; 1.
PROSITE; PS00196; COPPER_BLUE; 1.
PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Copper;
Direct protein sequencing; Electron transport; Glycoprotein; Membrane;
Metal-binding; Reference proteome; Signal; Transport.
SIGNAL 1 56 {ECO:0000255}.
PROPEP 57 80 {ECO:0000269|PubMed:1313011}.
/FTId=PRO_0000002846.
CHAIN 81 235 Auracyanin-B-1.
/FTId=PRO_0000002847.
CHAIN 89 235 Auracyanin-B-2.
/FTId=PRO_0000002848.
DOMAIN 111 235 Plastocyanin-like.
METAL 152 152 Copper.
METAL 217 217 Copper.
METAL 222 222 Copper.
METAL 227 227 Copper.
CONFLICT 183 183 P -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 186 186 P -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 219 219 F -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 223 226 YLAG -> TPI (in Ref. 3; AA sequence).
{ECO:0000305}.
STRAND 111 118 {ECO:0000244|PDB:1QHQ}.
STRAND 120 126 {ECO:0000244|PDB:1QHQ}.
STRAND 128 133 {ECO:0000244|PDB:1QHQ}.
STRAND 137 144 {ECO:0000244|PDB:1QHQ}.
STRAND 155 160 {ECO:0000244|PDB:1QHQ}.
HELIX 161 172 {ECO:0000244|PDB:1QHQ}.
HELIX 175 177 {ECO:0000244|PDB:1QHQ}.
STRAND 188 191 {ECO:0000244|PDB:1QHQ}.
STRAND 199 206 {ECO:0000244|PDB:1QHQ}.
STRAND 209 216 {ECO:0000244|PDB:1QHQ}.
TURN 220 226 {ECO:0000244|PDB:1QHQ}.
STRAND 228 234 {ECO:0000244|PDB:1QHQ}.
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


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