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Protein

Light-harvesting protein B-800/850 beta chain

Gene
N/A
Organism
Rhodoblastus acidophilus (Rhodopseudomonas acidophila)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi12 – 121Magnesium (bacteriochlorophyll axial ligand)Sequence Analysis
Metal bindingi30 – 301Magnesium (bacteriochlorophyll axial ligand)Sequence Analysis

GO - Molecular functioni

  1. bacteriochlorophyll binding Source: UniProtKB-KW
  2. electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. photosynthesis, light reaction Source: InterPro
  2. protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Light-harvesting polypeptide

Keywords - Ligandi

Bacteriochlorophyll, Chlorophyll, Chromophore, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Light-harvesting protein B-800/850 beta chain
Alternative name(s):
Antenna pigment protein beta chain
OrganismiRhodoblastus acidophilus (Rhodopseudomonas acidophila)
Taxonomic identifieri1074 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodoblastus

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1414CytoplasmicAdd
BLAST
Transmembranei15 – 3622HelicalAdd
BLAST
Topological domaini37 – 415Periplasmic

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
  3. plasma membrane light-harvesting complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Antenna complex, Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4141Light-harvesting protein B-800/850 beta chainPRO_0000099819Add
BLAST

Interactioni

Subunit structurei

The core complex is formed by different alpha and beta chains, binding bacteriochlorophyll molecules, and arranged most probably in tetrameric structures disposed around the reaction center. The non-pigmented gamma chains may constitute additional components.

Structurei

Secondary structure

1
41
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 3632Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZUX-ray2.50B/E/H1-41[»]
1NKZX-ray2.00B/D/F1-41[»]
2FKWX-ray2.45B/D/F/H/J/L/N/P/S1-41[»]
ProteinModelPortaliP26790.
SMRiP26790. Positions 1-41.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26790.

Family & Domainsi

Sequence similaritiesi

Belongs to the antena complex beta subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR000066. Antenna_a/b.
IPR002362. Antenna_beta.
IPR023623. Antenna_beta_CS.
[Graphical view]
PfamiPF00556. LHC. 1 hit.
[Graphical view]
PIRSFiPIRSF002900. Antenna_beta. 1 hit.
PRINTSiPR00674. LIGHTHARVSTB.
SUPFAMiSSF56918. SSF56918. 1 hit.
PROSITEiPS00969. ANTENNA_COMP_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26790-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40 
ATLTAEQSEE LHKYVIDGTR VFLGLALVAH FLAFSATPWL H
Length:41
Mass (Da):4,554
Last modified:August 1, 1992 - v1
Checksum:i60782AF6EA54CFD4
GO

Sequence databases

PIRiS07673.

Cross-referencesi

Sequence databases

PIRiS07673.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZUX-ray2.50B/E/H1-41[»]
1NKZX-ray2.00B/D/F1-41[»]
2FKWX-ray2.45B/D/F/H/J/L/N/P/S1-41[»]
ProteinModelPortaliP26790.
SMRiP26790. Positions 1-41.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP26790.

Family and domain databases

InterProiIPR000066. Antenna_a/b.
IPR002362. Antenna_beta.
IPR023623. Antenna_beta_CS.
[Graphical view]
PfamiPF00556. LHC. 1 hit.
[Graphical view]
PIRSFiPIRSF002900. Antenna_beta. 1 hit.
PRINTSiPR00674. LIGHTHARVSTB.
SUPFAMiSSF56918. SSF56918. 1 hit.
PROSITEiPS00969. ANTENNA_COMP_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete amino acid sequences of the B800-850 antenna polypeptides from Rhodopseudomonas acidophila strain 7750."
    Bissig I., Brunisholz R.A., Suter F., Cogdell R.J., Zuber H.
    Z. Naturforsch. C 43:77-83(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: DSM 141 / 7750 / LMG 4302.
  2. Brunisholz R.A., Bissig I., Niederer E., Suter F., Zuber H.
    (In) Biggins J. (eds.); Progress in photosynthesis research, pp.II.1:13-16, Martinus Nijhoff, The Hague (1987)
    Cited for: PROTEIN SEQUENCE.
    Strain: DSM 141 / 7750 / LMG 4302.
  3. "Apoprotein structure in the LH2 complex from Rhodopseudomonas acidophila strain 10050: modular assembly and protein pigment interactions."
    Prince S.M., Papiz M.Z., Freer A.A., McDermott G., Hawthornthwaite-Lawless A.M., Cogdell R.J., Isaacs N.W.
    J. Mol. Biol. 268:412-423(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    Strain: 10050.

Entry informationi

Entry nameiLHB5_RHOAC
AccessioniPrimary (citable) accession number: P26790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 7, 2015
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

External Data

Dasty 3

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 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.