(data stored in ACNUC7421 zone)

HOGENOM: THEEB_1_PE1013

ID   THEEB_1_PE1013                       STANDARD;      PRT;   81 AA.
AC   THEEB_1_PE1013; P0A415; P18083; P20451;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Photosystem I iron-sulfur center;AltName: Full=9 kDa
DE   polypeptide;AltName: Full=PSI-C;AltName: Full=Photosystem I subunit
DE   VII;AltName: Full=PsaC; (THEEB_1.PE1013).
GN   Name=psaC; OrderedLocusNames=tsl1013;
OS   THERMOSYNECHOCOCCUS ELONGATUS BP-1.
OC   Bacteria; Cyanobacteria; Chroococcales; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS THEEB_1.PE1013.
CC       Thermosynechococcus elongatus BP-1, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:PSAC_THEEB
CC   -!- FUNCTION: Apoprotein for the two 4Fe-4S centers FA and FB of
CC       photosystem I (PSI); essential for photochemical activity. FB is
CC       the terminal electron acceptor of PSI, donating electrons to
CC       ferredoxin. The C-terminus interacts with psaA/B/D and helps
CC       assemble the protein into the PSI complex. Required for binding of
CC       psaD and psaE to PSI. PSI is a plastocyanin/cytochrome c6-
CC       ferredoxin oxidoreductase, converting photonic excitation into a
CC       charge separation, which transfers an electron from the donor P700
CC       chlorophyll pair to the spectroscopically characterized acceptors
CC       A0, A1, FX, FA and FB in turn.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters. Cluster 2 is most probably the
CC       spectroscopically characterized electron acceptor FA and cluster 1
CC       is most probably FB (By similarity).
CC   -!- SUBUNIT: The cyanobacterial PSI reaction center is composed of one
CC       copy each of psaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric
CC       complexes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
CC   -!- GENE_FAMILY: HOG000230505 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; P0A415; P18083; P20451; -.
DR   EMBL; BA000039; BAC08565.1; -; Genomic_DNA.
DR   RefSeq; NP_681803.1; NC_004113.1.
DR   PDB; 1C51; X-ray; 4.0 A; -.
DR   PDB; 1JB0; X-ray; 2.50 A; C=2-81.
DR   PDB; 2PPS; X-ray; 4.0 A; -.
DR   PDB; 3PCQ; X-ray; 8.98 A; C=2-81.
DR   PDBsum; 1C51; -.
DR   PDBsum; 1JB0; -.
DR   PDBsum; 2PPS; -.
DR   PDBsum; 3PCQ; -.
DR   ProteinModelPortal; P0A415; -.
DR   SMR; P0A415; 2-81.
DR   STRING; P0A415; -.
DR   GeneID; 1011306; -.
DR   GenomeReviews; BA000039_GR; tsl1013.
DR   KEGG; tel:tsl1013; -.
DR   NMPDR; fig|197221.1.peg.1012; -.
DR   eggNOG; COG1145; -.
DR   OMA; EDCIGCK; -.
DR   ProtClustDB; PRK02651; -.
DR   BioCyc; TELO197221:TSL1013-MON; -.
DR   GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
DR   GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009773; P:photosynthetic electron transport in photosystem I; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   HAMAP; MF_01303; PSI_PsaC; 1; -.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR017491; PSI_PsaC.
DR   TIGRFAMs; TIGR03048; PS_I_psaC; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
DR   HOGENOMDNA; THEEB_1.PE1013; -.
KW   photosystem I subunit VII;
KW   3D-structure; 4Fe-4S; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Photosynthesis; Photosystem I;
KW   Reference proteome; Repeat; Thylakoid; Transport.
SQ   SEQUENCE   81 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAHTVKIYDT CIGCTQCVRA CPTDVLEMVP WDGCKAGQIA SSPRTEDCVG CKRCETACPT
     DFLSIRVYLG AETTRSMGLA Y
//

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