Photosystem Q(B) protein precursor - Synechocystis sp. (strain PCC 6714)

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P14660 (PSBA_SYNY4) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 82. History...

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

Documents (1) |

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
EC=1.10.3.9

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

Gene names

Name:	psbA
Synonyms:	psbA-I

Organism

Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714))

Taxonomic identifier

1147 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › 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 MF_01379
Catalytic activity	2 H₂O + 2 plastoquinone + 4 light = O₂ + 2 plastoquinol. HAMAP 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 MF_01379.
Miscellaneous	Herbicides such as atrazine, BNT, diuron or ioxynil bind to Q(B) and block electron transport. HAMAP MF_01379 Cyanobacteria usually contain more than 2 copies of the psbA gene. HAMAP 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
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 transport 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 photosystem II Inferred from electronic annotation. Source: UniProtKB-KW 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 metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 HAMAP MF_01379

PRO_0000090494

Propeptide

345 – 360

Potential

PRO_0000316427

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

211

F → S: Az-V; herbicide resistance.

Mutagenesis

251

A → V: Az-V; herbicide resistance.

Mutagenesis

255

F → L: DCMU-IIA; herbicide resistance.

Mutagenesis

264

S → A: DCMU-IIA/B; herbicide resistance.

Mutagenesis

266

N → D: IoxIIA; herbicide resistance.

Mutagenesis

266

N → T: IoxI; herbicide resistance.

Sequences

Sequence

Length

Mass (Da)

Tools

P14660 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 8B8D917DC9C840B6
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FASTA

360

39,812

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

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

       130        140        150        160        170        180 
IGIFCYMGRQ WELSYRLGMR PWICVAYSAP VSARTAVFLI 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 VALTAPAING

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References

[1]	"Molecular analysis of psbA mutations responsible for various herbicide resistance phenotypes in Synechocystis 6714." Ajlani G., Kirilovsky D., Picaud M., Astier C. Plant Mol. Biol. 13:469-479(1989) [PubMed: 2518834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANTS.
[2]	"Mutation in phenol-type herbicide resistance maps within the psbA gene in Synechocystis 6714." Ajlani G., Meyer I., Vernotte C., Astier C. FEBS Lett. 246:207-210(1989) [PubMed: 2495986] [Abstract] Cited for: MUTANT IOXI THR-266.
[3]	"A new ioxynil-resistant mutant in Synechocystis PCC 6714: hypothesis on the interaction of ioxynil with the D 1 protein." Creuzet S., Ajlani G., Vernotte C., Astier C. Z. Naturforsch. C 45:436-440(1990) [PubMed: 2116129] [Abstract] Cited for: MUTANT IOXIIA ASP-266.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X15514 Genomic DNA. Translation: CAA33538.1.
PIR	F2YB17. S07461.
3D structure databases
ProteinModelPortal	P14660.
SMR	P14660. Positions 10-344.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
HAMAP	MF_01379. PSII_PsbA_D1. [Tree]
InterPro	IPR000484. Photo_RC_L/M. IPR005867. PSII_PsbA/D1. [Graphical view]
Gene3D	G3DSA:1.20.85.10. Photo_RC_L/M. 1 hit.
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

PSBA_SYNY4

Accession

Primary (citable) accession number: P14660

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	October 19, 2011
This is version 82 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

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

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents