ID K9ZDS6_ANACC Unreviewed; 360 AA.
AC K9ZDS6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 16-OCT-2013, entry version 6.
DE RecName: Full=Photosystem Q(B) protein;
DE EC=1.10.3.9;
DE AltName: Full=32 kDa thylakoid membrane protein;
DE AltName: Full=Photosystem II protein D1;
DE Flags: Precursor;
GN Name=psbA; OrderedLocusNames=Anacy_0955, Anacy_5146;
OS Anabaena cylindrica (strain ATCC 27899 / PCC 7122).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=272123;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7122;
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A.,
RA Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Pagani I., Pati A., Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X.,
RA Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Anabaena cylindrica PCC 7122.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27899 / PCC 7122;
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E.,
RA Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-
RT driven genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- FUNCTION: This is one of the two reaction center proteins of
CC photosystem II (PSII) (By similarity).
CC -!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
CC plastoquinol.
CC -!- COFACTOR: The PsbA/B heterodimer binds P680, the primary electron
CC donor of PSII. It shares a non-heme iron and each subunit binds
CC additional chlorophylls and pheophytin. PsbA provides most of the
CC ligands for the Mn-cluster of the oxygen-evolving complex (By
CC similarity).
CC -!- SUBUNIT: The PsbA/B heterodimer binds the P680 chlorophylls and
CC subsequent electron acceptors. PSII consists of a core antenna
CC complex that captures photons and an electron transfer chain that
CC converts photonic excitation into a charge separation. PSII forms
CC dimeric complexes (By similarity).
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Multi-pass
CC membrane protein (By similarity).
CC -!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of
CC the psbA gene (By similarity).
CC -!- MISCELLANEOUS: Herbicides such as atrazine, BNT, diuron or ioxynil
CC bind to Q(B) and block electron transport (By similarity).
CC -!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
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DR EMBL; CP003659; AFZ56530.1; -; Genomic_DNA.
DR EMBL; CP003659; AFZ60480.1; -; Genomic_DNA.
DR RefSeq; YP_007155440.1; NC_019771.1.
DR RefSeq; YP_007159390.1; NC_019771.1.
DR GeneID; 14187052; -.
DR GeneID; 14187493; -.
DR KEGG; acy:Anacy_0955; -.
DR KEGG; acy:Anacy_5146; -.
DR KO; K02703; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
DR GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
DR GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
DR Gene3D; 1.20.85.10; -; 1.
DR HAMAP; MF_01379; PSII_PsbA_D1; 1; -.
DR InterPro; IPR000484; Photo_RC_L/M.
DR InterPro; IPR005867; PSII_D1.
DR Pfam; PF00124; Photo_RC; 1.
DR PRINTS; PR00256; REACTNCENTRE.
DR SUPFAM; SSF81483; SSF81483; 1.
DR TIGRFAMs; TIGR01151; psbA; 1.
DR PROSITE; PS00244; REACTION_CENTER; 1.
PE 3: Inferred from homology;
KW Calcium; Complete proteome; Electron transport; Herbicide resistance;
KW Iron; Manganese; Membrane; Metal-binding; Oxidoreductase;
KW Photosynthesis; Photosystem II; Signal; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 43 Potential.
FT CHAIN 44 360 Potential.
FT /FTId=PRO_5001084280.
FT TRANSMEM 36 56 Helical; (By similarity).
FT TRANSMEM 109 129 Helical; (By similarity).
FT TRANSMEM 141 164 Helical; (By similarity).
FT TRANSMEM 192 218 Helical; (By similarity).
FT TRANSMEM 269 289 Helical; (By similarity).
FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; calcium (By similarity).
FT METAL 170 170 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 1 (By similarity).
FT METAL 189 189 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 2 (By similarity).
FT METAL 215 215 Iron; shared with heterodimeric partner
FT (By similarity).
FT METAL 272 272 Iron; shared with heterodimeric partner
FT (By similarity).
FT METAL 332 332 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 2; via tele nitrogen (By
FT similarity).
FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 1 (By similarity).
FT METAL 333 333 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 3 (By similarity).
FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 2 (By similarity).
FT METAL 342 342 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 4 (By similarity).
FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; calcium; via carboxylate (By
FT similarity).
FT METAL 344 344 Calcium-manganese-oxide cluster [Ca-4Mn-
FT 5O]; manganese 4; via carboxylate (By
FT similarity).
FT SITE 344 345 Cleavage; by CtpA (By similarity).
SQ SEQUENCE 360 AA; 39593 MW; B12899D31245F23C CRC64;
MTTTIQQRST ANVWDRFCEW ITSTENRIYI GWFGVLMIPT LLAATTCFII AFIAAPPVDI
DGIREPVAGS LIYGNNIISG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLVIFHFL
IGCACYLGRQ WELSYRLGMR PWICVAYSAP LASATAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLVRETTET ESQNYGYKFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV IGIWFTALGV STMAFNLNGF
NFNQSIIDSQ GRVIGTWADV INRANLGMEV MHERNAHNFP LDLAAGDVAP VALTAPAING
//