Photosystem Q(B) protein 2 precursor - Synechocystis sp. (strain PCC 6803 / Kazusa)

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P16033 (PSBA2_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 114. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Photosystem Q(B) protein 2
EC=1.10.3.9

Alternative name(s):
32 kDa thylakoid membrane protein 2
Photosystem II protein D1 2

Gene names

Name:	psbA2
Synonyms:	psbA-2
Ordered Locus Names:	slr1311
AND
Name:	psbA3
Synonyms:	psbA-3
Ordered Locus Names:	sll1867

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP]

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis ›

Protein attributes

Sequence length	360 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	This is one of the two reaction center proteins of photosystem II By similarity. HAMAP-Rule MF_01379
Catalytic activity	2 H₂O + 2 plastoquinone + 4 light = O₂ + 2 plastoquinol. HAMAP-Rule MF_01379
Cofactor	The PsbA/B heterodimer binds P680, the primary electron donor of PSII. It shares a non-heme iron and each subunit binds additional chlorophylls and pheophytin. PsbA provides most of the ligands for the Mn-cluster of the oxygen-evolving complex By similarity.
Subunit structure	The PsbA/B heterodimer binds the P680 chlorophylls and subsequent electron acceptors. PSII consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes By similarity.
Subcellular location	Cellular thylakoid membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01379.
Miscellaneous	Herbicides such as atrazine, BNT, diuron or ioxynil bind to Q(B) and block electron transport. HAMAP-Rule MF_01379 Cyanobacteria usually contain more than 2 copies of the psbA gene. HAMAP-Rule MF_01379
Sequence similarities	Belongs to the reaction center PufL/M/PsbA/D family.

Ontologies

Keywords
Biological process	Electron transport Herbicide resistance Photosynthesis Transport
Cellular component	Membrane Photosystem II Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	photosynthetic electron transport in photosystem II Inferred from electronic annotation. Source: InterPro response to herbicide Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW light-harvesting complex Inferred from electronic annotation. Source: InterPro plasma membrane-derived thylakoid photosystem II Inferred from direct assay PubMed 12069591 PubMed 14730074. Source: UniProtKB thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP oxidoreductase activity 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 – 344

344

Photosystem Q(B) protein 2 HAMAP-Rule MF_01379

PRO_0000090493

Propeptide

345 – 360

Potential

PRO_0000316429

Regions

Transmembrane

36 – 56

Helical; Potential

Transmembrane

109 – 129

Helical; Potential

Transmembrane

141 – 164

Helical; Potential

Transmembrane

192 – 218

Helical; Potential

Transmembrane

269 – 289

Helical; Potential

Sites

Metal binding

215

Iron; shared with heterodimeric partner By similarity

Metal binding

272

Iron; shared with heterodimeric partner By similarity

Site

344 – 345

Cleavage; by CtpA By similarity

Experimental info

Mutagenesis

221 – 222

SS → LA: Strong herbicide resistance.

Mutagenesis

227 – 228

TT → AA: Herbicide resistance.

Mutagenesis

237

Y → F: Weak herbicide resistance.

Mutagenesis

238

K → V: Weak herbicide resistance.

Mutagenesis

255

F → W: Herbicide resistance.

Mutagenesis

257

R → V: Herbicide resistance.

Mutagenesis

264

S → A: Strong herbicide resistance.

Mutagenesis

271

L → V, M, A or S: Herbicide resistance.

Sequences

Sequence

Length

Mass (Da)

Tools

P16033 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 2FE4088498A416C2
Show »

FASTA

360

39,721

        10         20         30         40         50         60 
MTTTLQQRES ASLWEQFCQW VTSTNNRIYV GWFGTLMIPT LLTATTCFII AFIAAPPVDI 

        70         80         90        100        110        120 
DGIREPVAGS LLYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVVFHFL 

       130        140        150        160        170        180 
IGIFCYMGRQ WELSYRLGMR PWICVAYSAP VSAATAVFLI YPIGQGSFSD GMPLGISGTF 

       190        200        210        220        230        240 
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTEV ESQNYGYKFG 

       250        260        270        280        290        300 
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLGAWPV IGIWFTAMGV STMAFNLNGF 

       310        320        330        340        350        360 
NFNQSILDSQ GRVIGTWADV LNRANIGFEV MHERNAHNFP LDLASGEQAP VALTAPAVNG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a second psbA gene from the unicellular cyanobacterium Synechocystis 6803." Ravnikar P.D., Debus R., Sevrinck J., Saetaert P., McIntosh L. Nucleic Acids Res. 17:3991-3991(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the psbA3 gene from the cyanobacterium Synechocystis PCC 6803." Metz J., Nixon P., Diner B. Nucleic Acids Res. 18:6715-6715(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S. DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa.
[4]	"Mutations in the D1 subunit of photosystem II distinguish between quinone and herbicide binding sites." Ohad N., Hirschberg J. Plant Cell 4:273-282(1992) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS FOR HERBICIDE RESISTANCE.
[5]	"The D-E region of the D1 protein is involved in multiple quinone and herbicide interactions in photosystem II." Kless H., Oren-Shamir M., Malkin S., McIntosh L., Edelman M. Biochemistry 33:10501-10507(1994) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS FOR HERBICIDE RESISTANCE.
[6]	"Thylakoid protein phosphorylation in evolutionally divergent species with oxygenic photosynthesis." Pursiheimo S., Rintamaeki E., Baena-Gonzalez E., Aro E.-M. FEBS Lett. 423:178-182(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ABSENCE OF PHOSPHORYLATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X56000 Genomic DNA. Translation: CAA39472.1. X13547 Genomic DNA. Translation: CAA31899.1. BA000022 Genomic DNA. Translation: BAA18230.1. BA000022 Genomic DNA. Translation: BAA16586.1.
PIR	F2YB16. S13112.
RefSeq	NP_439906.1. NC_000911.1. NP_441550.1. NC_000911.1. YP_005649961.1. NC_017277.1. YP_005651608.1. NC_017277.1. YP_007449789.1. NC_020286.1. YP_007451432.1. NC_020286.1.
3D structure databases
ProteinModelPortal	P16033.
SMR	P16033. Positions 10-344.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16033. 5 interactions.
STRING	1148.slr1311.
Protein family/group databases
TCDB	3.E.2.2.2. photosynthetic reaction center (PRC) family.
Proteomic databases
PaxDb	P16033.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAA16586; BAA16586; BAA16586. BAA18230; BAA18230; BAA18230.
GeneID	12254260. 12255303. 14615430. 14617092. 951890. 953105.
KEGG	syn:sll1867. syn:slr1311. syy:SYNGTS_0008. syy:SYNGTS_1655.
PATRIC	23836870. VBISynSp132158_0010.
Phylogenomic databases
eggNOG	NOG04871.
HOGENOM	HOG000246913.
KO	K02703.
OMA	CFTIAFI.
ProtClustDB	CLSK892431.
Family and domain databases
Gene3D	1.20.85.10. 1 hit.
HAMAP	MF_01379. PSII_PsbA_D1.
InterPro	IPR000484. Photo_RC_L/M. IPR005867. PSII_D1. [Graphical view]
Pfam	PF00124. Photo_RC. 1 hit. [Graphical view]
PRINTS	PR00256. REACTNCENTRE.
SUPFAM	SSF81483. Photo_RC_L/M. 1 hit.
TIGRFAMs	TIGR01151. psbA. 1 hit.
PROSITE	PS00244. REACTION_CENTER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSBA2_SYNY3

Accession

Primary (citable) accession number: P16033

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents