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Protein

Light-harvesting protein B-875 beta chain

Gene

pufB

Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi21 – 211Magnesium (bacteriochlorophyll axial ligand)
Metal bindingi39 – 391Magnesium (bacteriochlorophyll axial ligand)

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-875 beta chain
Alternative name(s):
Antenna pigment protein beta chain
LH-3A
Gene namesi
Name:pufB
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 2726CytoplasmicAdd
BLAST
Transmembranei28 – 4518Helical; Signal-anchor for type II membrane proteinAdd
BLAST
Topological domaini46 – 494Periplasmic

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
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 4948Light-harvesting protein B-875 beta chainPRO_0000099833Add
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
49
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources
Helixi9 – 2012Combined sources
Helixi22 – 3110Combined sources
Helixi34 – 4411Combined sources
Turni46 – 483Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DX7NMR-A2-49[»]
1JO5NMR-A2-49[»]
ProteinModelPortaliP0C0Y1.
SMRiP0C0Y1. Positions 2-49.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0Y1.

Family & Domainsi

Sequence similaritiesi

Belongs to the antena complex beta subunit family.Curated

Keywords - Domaini

Signal-anchor, 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.

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

P0C0Y1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40 
MADKSDLGYT GLTDEQAQEL HSVYMSGLWP FSAVAIVAHL AVYIWRPWF
Length:49
Mass (Da):5,572
Last modified:January 23, 2007 - v2
Checksum:i8C5B2F647A157582
GO

Sequence databases

PIRiB27760. LBRFAS.

Cross-referencesi

Sequence databases

PIRiB27760. LBRFAS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DX7NMR-A2-49[»]
1JO5NMR-A2-49[»]
ProteinModelPortaliP0C0Y1.
SMRiP0C0Y1. Positions 2-49.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0Y1.

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 light-harvesting polypeptides of Rhodopseudomonas sphaeroides R-26.1. I. Isolation, purification and sequence analyses."
    Theiler R., Suter F., Wiemken V., Zuber H.
    Hoppe-Seyler's Z. Physiol. Chem. 365:703-719(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-49.
    Strain: R-26.1.
  2. "The solution structure of Rhodobacter sphaeroides LH1beta reveals two helical domains separated by a more flexible region: structural consequences for the LH1 complex."
    Conroy M.J., Westerhuis W.H.J., Parkes-Loach P.S., Loach P.A., Hunter C.N., Williamson M.P.
    J. Mol. Biol. 298:83-94(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
    Strain: DD13.

Entry informationi

Entry nameiLHB1_RHOSH
AccessioniPrimary (citable) accession number: P0C0Y1
Secondary accession number(s): P02951
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 48 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, 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.