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Protein

Auracyanin-B

Gene

Caur_1950

Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably a soluble electron acceptor for the integral membrane protein electron transfer alternative complex III (ACIII).1 Publication

Cofactori

Cu cationNote: Binds 1 copper ion per subunit.

Redox potential

E0 is +190 mV at pH 9, +215 mV at pH 7 and +240 mV at pH 4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi152 – 1521Copper
Metal bindingi217 – 2171Copper
Metal bindingi222 – 2221Copper
Metal bindingi227 – 2271Copper

GO - Molecular functioni

  • copper ion binding Source: UniProtKB
  • electron carrier activity Source: InterPro

GO - Biological processi

  • photosynthetic electron transport chain Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

Copper, Metal-binding

Enzyme and pathway databases

BioCyciCAUR324602:GIXU-1976-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Auracyanin-B
Short name:
Ac-B
Cleaved into the following 2 chains:
Gene namesi
Ordered Locus Names:Caur_1950
OrganismiChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Taxonomic identifieri324602 [NCBI]
Taxonomic lineageiBacteriaChloroflexiChloroflexiaChloroflexalesChloroflexineaeChloroflexaceaeChloroflexus
Proteomesi
  • UP000002008 Componenti: Chromosome

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

  • Note: Possibly located on the extracellular face of the cell membrane.

GO - Cellular componenti

  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5656Sequence analysisAdd
BLAST
Propeptidei57 – 80241 PublicationPRO_0000002846Add
BLAST
Chaini81 – 235155Auracyanin-B-1PRO_0000002847Add
BLAST
Chaini89 – 235147Auracyanin-B-2PRO_0000002848Add
BLAST

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Expressioni

Inductioni

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).3 Publications

Interactioni

Protein-protein interaction databases

STRINGi324602.Caur_1950.

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi111 – 1188Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi128 – 1336Combined sources
Beta strandi137 – 1448Combined sources
Beta strandi155 – 1606Combined sources
Helixi161 – 17212Combined sources
Helixi175 – 1773Combined sources
Beta strandi188 – 1914Combined sources
Beta strandi199 – 2068Combined sources
Beta strandi209 – 2168Combined sources
Turni220 – 2267Combined sources
Beta strandi228 – 2347Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OV8X-ray1.90A/B/C/D96-235[»]
1QHQX-ray1.55A96-235[»]
ProteinModelPortaliP27197.
SMRiP27197. Positions 97-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27197.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 235125Plastocyanin-likeAdd
BLAST

Sequence similaritiesi

Belongs to the multicopper oxidase family.Curated
Contains 1 plastocyanin-like domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105UTB. Bacteria.
COG3241. LUCA.
HOGENOMiHOG000034233.
InParanoidiP27197.
OMAiHYLAGMK.
OrthoDBiEOG6G20MV.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
PS00079. MULTICOPPER_OXIDASE1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27197-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWRGSGRSN FRSRSSSNGG STFSGGSAGG PPLIVMMGLA FGAGLIMLIV
60 70 80 90 100
MIASNATAGG FVAATPRPTA TPRPTAAPAP TQPPAAQPTT APATQAANAP
110 120 130 140 150
GGSNVVNETP AQTVEVRAAP DALAFAQTSL SLPANTVVRL DFVNQNNLGV
160 170 180 190 200
QHNWVLVNGG DDVAAAVNTA AQNNADALFV PPPDTPNALA WTAMLNAGES
210 220 230
GSVTFRTPAP GTYLYICTFP GHYLAGMKGT LTVTP
Length:235
Mass (Da):23,716
Last modified:November 1, 1997 - v2
Checksum:i845186230C072521
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti183 – 1831P → G AA sequence (PubMed:1313011).Curated
Sequence conflicti186 – 1861P → A AA sequence (PubMed:1313011).Curated
Sequence conflicti219 – 2191F → G AA sequence (PubMed:1313011).Curated
Sequence conflicti223 – 2264YLAG → TPI AA sequence (PubMed:1313011).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78046 Genomic DNA. Translation: AAB38318.1.
CP000909 Genomic DNA. Translation: ABY35165.1.
RefSeqiWP_012257819.1. NC_010175.1.
YP_001635554.1. NC_010175.1.

Genome annotation databases

EnsemblBacteriaiABY35165; ABY35165; Caur_1950.
GeneIDi5826401.
KEGGicau:Caur_1950.
PATRICi21414911. VBIChlAur28763_2219.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U78046 Genomic DNA. Translation: AAB38318.1.
CP000909 Genomic DNA. Translation: ABY35165.1.
RefSeqiWP_012257819.1. NC_010175.1.
YP_001635554.1. NC_010175.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OV8X-ray1.90A/B/C/D96-235[»]
1QHQX-ray1.55A96-235[»]
ProteinModelPortaliP27197.
SMRiP27197. Positions 97-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi324602.Caur_1950.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABY35165; ABY35165; Caur_1950.
GeneIDi5826401.
KEGGicau:Caur_1950.
PATRICi21414911. VBIChlAur28763_2219.

Phylogenomic databases

eggNOGiENOG4105UTB. Bacteria.
COG3241. LUCA.
HOGENOMiHOG000034233.
InParanoidiP27197.
OMAiHYLAGMK.
OrthoDBiEOG6G20MV.

Enzyme and pathway databases

BioCyciCAUR324602:GIXU-1976-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP27197.

Family and domain databases

Gene3Di2.60.40.420. 1 hit.
InterProiIPR000923. BlueCu_1.
IPR028871. BlueCu_1_BS.
IPR033138. Cu_oxidase_CS.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00127. Copper-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 1 hit.
PROSITEiPS00196. COPPER_BLUE. 1 hit.
PS00079. MULTICOPPER_OXIDASE1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene sequence for auracyanin B from Chloroflexus aurantiacus."
    Lopez J.C., Dracheva S., Blankenship R.E.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29366 / DSM 635 / J-10-fl.
  3. "Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus."
    McManus J.D., Brune D.C., Han J., Sanders-Loehr J., Meyer T.E., Cusanovich M.A., Tollin G., Blankenship R.E.
    J. Biol. Chem. 267:6531-6540(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 81-235, FUNCTION, COPPER BINDING, SUBCELLULAR LOCATION, GLYCOSYLATION.
  4. "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."
    Rooney M.B., Honeychurch M.J., Selvaraj F.M., Blankenship R.E., Bond A.M., Freeman H.C.
    J. Biol. Inorg. Chem. 8:306-317(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
  5. "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."
    Lee M., del Rosario M.C., Harris H.H., Blankenship R.E., Guss J.M., Freeman H.C.
    J. Biol. Inorg. Chem. 14:329-345(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC 29366 / DSM 635 / J-10-fl.
  6. "Comparison of Chloroflexus aurantiacus strain J-10-fl proteomes of cells grown chemoheterotrophically and photoheterotrophically."
    Cao L., Bryant D.A., Schepmoes A.A., Vogl K., Smith R.D., Lipton M.S., Callister S.J.
    Photosyn. Res. 110:153-168(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Alternative Complex III from phototrophic bacteria and its electron acceptor auracyanin."
    Majumder E.L., King J.D., Blankenship R.E.
    Biochim. Biophys. Acta 1827:1383-1391(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "Crystal structure of auracyanin, a 'blue' copper protein from the green thermophilic photosynthetic bacterium Chloroflexus aurantiacus."
    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.
    J. Mol. Biol. 306:47-67(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 81-235.

Entry informationi

Entry nameiAURB_CHLAA
AccessioniPrimary (citable) accession number: P27197
Secondary accession number(s): A9WE06, P94610
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1997
Last modified: March 16, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.