P02947 (LHA_RHORU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Light-harvesting protein B-870 alpha chain Alternative name(s): Antenna pigment protein alpha chain LH-1
Organism	Rhodospirillum rubrum
Taxonomic identifier	1085 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Rhodospirillaceae › Rhodospirillum

Protein attributes

Sequence length	62 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers.
Subunit structure	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.
Subcellular location	Cell inner membrane; Single-pass type II membrane protein.
Sequence similarities	Belongs to the antena complex alpha subunit family.

Ontologies

Keywords
Cellular component	Antenna complex Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Bacteriochlorophyll Chlorophyll Chromophore Magnesium Metal-binding
Molecular function	Light-harvesting polypeptide
PTM	Formylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	photosynthesis, light reaction Inferred from electronic annotation. Source: InterPro protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW organelle inner membrane Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane light-harvesting complex Inferred from electronic annotation. Source: InterPro
Molecular_function	bacteriochlorophyll binding Inferred from electronic annotation. Source: UniProtKB-KW electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 52

52

Light-harvesting protein B-870 alpha chain

PRO_0000001625

Propeptide

53 – 62

10

PRO_0000001626

Regions

Topological domain

1 – 12

12

Cytoplasmic Potential

Transmembrane

13 – 33

21

Helical; Potential

Topological domain

34 – 52

19

Periplasmic Potential

Sites

Metal binding

29

1

Magnesium (bacteriochlorophyll axial ligand) Potential

Amino acid modifications

Modified residue

1

1

N-formylmethionine Probable

Secondary structure

1

.

.

.

.

.

.

.

62

Helix Strand Turn

Details...

Helix

2 – 6

5

Helix

10 – 42

33

Beta strand

44 – 48

5

Sequences

	Sequence		Length	Mass (Da)
	P02947 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 66DB6F8513347090	FASTA	62	7,107
	10 20 30 40 50 60 MWRIWQLFDP RQALVGLATF LFVLALLIHF ILLSTERFNW LEGASTKPVQ TSMVMPSSDL AV

References

[1]	"Molecular cloning and sequence of the B880 holochrome gene from Rhodospirillum rubrum." Berard J., Belanger G., Corriveau P., Gingras G. J. Biol. Chem. 261:82-87(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete amino acid sequence of the single light harvesting protein from chromatophores of Rhodospirillum rubrum G9(+)." Brunisholz R.A., Cuendet P.A., Theiler R., Zuber H. FEBS Lett. 129:150-154(1981) Cited for: PROTEIN SEQUENCE OF 1-52, FORMYLATION AT MET-1. Strain: G-9+.
[3]	"Solution structures of the core light-harvesting alpha and beta polypeptides from Rhodospirillum rubrum: implications for the pigment-protein and protein-protein interactions." Wang Z.Y., Gokan K., Kobayashi M., Nozawa T. J. Mol. Biol. 347:465-477(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-52.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M11801 Genomic DNA. Translation: AAA26462.1.

PIR

LBQFR. B24206.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NW0	model	-	A	1-52	[»]
1XRD	NMR	-	A	1-52	[»]

ProteinModelPortal

P02947.

SMR

P02947. Positions 1-52.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000066. Antenna_a/b.
IPR018332. Antenna_alpha.
IPR002361. Antenna_alpha_CS.
[Graphical view]

Pfam

PF00556. LHC. 1 hit.
[Graphical view]

PRINTS

PR00673. LIGHTHARVSTA.

SUPFAM

SSF56918. Antenna_a/b. 1 hit.

PROSITE

PS00968. ANTENNA_COMP_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02947.

Entry information

Entry name

LHA_RHORU

Accession

Primary (citable) accession number: P02947

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 1, 1988
Last modified:	April 3, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program