ID   AURA_CHLAA              Reviewed;         162 AA.
AC   Q8RMH6; A9WIX7; Q3DWS6; Q7M1C1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Auracyanin-A;
DE   Flags: Precursor;
GN   OrderedLocusNames=Caur_3248;
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] {ECO:0000305, ECO:0000312|EMBL:AAM12874.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl {ECO:0000312|EMBL:AAM12874.1};
RA   Blankenship R.E., Lince M.T., Hiller R.G.;
RL   Submitted (MAR-2002) 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] {ECO:0000305, ECO:0000312|PIR:B42418}
RP   PROTEIN SEQUENCE OF 23-162, AND MASS SPECTROMETRY.
RX   PubMed=10338005; DOI=10.1110/ps.8.5.947;
RA   Van Driessche G., Hu W., Van de Werken G., Selvaraj F., McManus J.D.,
RA   Blankenship R.E., Van Beeumen J.J.;
RT   "Auracyanin A from the thermophilic green gliding photosynthetic bacterium
RT   Chloroflexus aurantiacus represents an unusual class of small blue copper
RT   proteins.";
RL   Protein Sci. 8:947-957(1999).
RN   [4] {ECO:0000305}
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, 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   [6]
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   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 40-162 IN COMPLEX WITH COPPER,
RP   COFACTOR, SUBUNIT, AND 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).
CC   -!- FUNCTION: Probably a soluble electron acceptor for the integral
CC       membrane protein electron transfer alternative complex III (ACIII).
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000269|PubMed:19190939};
CC       Note=Binds 1 copper ion per subunit. {ECO:0000269|PubMed:19190939};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +190 mV at pH 9, +205 mV at pH 7 and +240 mV at pH 4.
CC         {ECO:0000269|PubMed:12589566};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19190939}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}. Note=Possibly located on the extracellular face of the
CC       cell membrane.
CC   -!- INDUCTION: Present in photosynthetically (anaerobically) but not dark
CC       (aerobic respiration) grown cells (at protein level). Apparently
CC       unprocessed protein is also present, its quantities increase with
CC       culture age (PubMed:19190939). A later paper showed this protein to be
CC       present in both chemoheterotrophically (dark) and
CC       photoheterotrophically (light) grown cells, but with more protein
CC       present in dark grown cells (PubMed:22249883). The second report is
CC       thought to be correct (PubMed:23357331). {ECO:0000269|PubMed:19190939,
CC       ECO:0000269|PubMed:22249883, ECO:0000269|PubMed:23357331}.
CC   -!- MASS SPECTROMETRY: Mass=14128; Method=FAB;
CC       Evidence={ECO:0000269|PubMed:10338005};
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000255}.
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DR   EMBL; AF494277; AAM12874.1; -; Genomic_DNA.
DR   EMBL; CP000909; ABY36436.1; -; Genomic_DNA.
DR   PIR; B42418; B42418.
DR   RefSeq; WP_012259089.1; NC_010175.1.
DR   RefSeq; YP_001636825.1; NC_010175.1.
DR   PDB; 2AAN; X-ray; 1.85 A; A=24-162.
DR   PDBsum; 2AAN; -.
DR   AlphaFoldDB; Q8RMH6; -.
DR   SMR; Q8RMH6; -.
DR   STRING; 324602.Caur_3248; -.
DR   EnsemblBacteria; ABY36436; ABY36436; Caur_3248.
DR   KEGG; cau:Caur_3248; -.
DR   PATRIC; fig|324602.8.peg.3667; -.
DR   eggNOG; COG3241; Bacteria.
DR   HOGENOM; CLU_112845_2_0_0; -.
DR   InParanoid; Q8RMH6; -.
DR   OMA; MGHNFVL; -.
DR   EvolutionaryTrace; Q8RMH6; -.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
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; IPR008972; Cupredoxin.
DR   Pfam; PF00127; Copper-bind; 1.
DR   SUPFAM; SSF49503; SSF49503; 1.
DR   PROSITE; PS00196; COPPER_BLUE; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Copper; Direct protein sequencing;
KW   Electron transport; Lipoprotein; Membrane; Metal-binding; Palmitate;
KW   Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT                   ECO:0000269|PubMed:10338005"
FT   CHAIN           23..162
FT                   /note="Auracyanin-A"
FT                   /id="PRO_0000252039"
FT   DOMAIN          42..162
FT                   /note="Plastocyanin-like"
FT                   /evidence="ECO:0000255"
FT   BINDING         81
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:19190939"
FT   BINDING         146
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:19190939"
FT   BINDING         151
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:19190939"
FT   BINDING         155
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /evidence="ECO:0000269|PubMed:19190939"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          58..63
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          67..73
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          84..88
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   HELIX           90..103
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          117..120
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          129..135
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          138..145
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   TURN            149..154
FT                   /evidence="ECO:0007829|PDB:2AAN"
FT   STRAND          155..162
FT                   /evidence="ECO:0007829|PDB:2AAN"
SQ   SEQUENCE   162 AA;  16371 MW;  558A7B9F85AC2828 CRC64;
     MKITLRMMVL AVLTAMAMVL AACGGGGSSG GSTGGGSGSG PVTIEIGSKG EELAFDKTEL
     TVSAGQTVTI RFKNNSAVQQ HNWILVKGGE AEAANIANAG LSAGPAANYL PADKSNIIAE
     SPLANGNETV EVTFTAPAAG TYLYICTVPG HYPLMQGKLV VN