GenomeNet

Database: UniProt
Entry: Q8DHJ2
LinkDB: Q8DHJ2
Original site: Q8DHJ2 
ID   PSBZ_THEEB              Reviewed;          62 AA.
AC   Q8DHJ2;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   07-APR-2021, entry version 119.
DE   RecName: Full=Photosystem II reaction center protein Z {ECO:0000255|HAMAP-Rule:MF_00644};
DE            Short=PSII-Z {ECO:0000255|HAMAP-Rule:MF_00644};
GN   Name=psbZ {ECO:0000255|HAMAP-Rule:MF_00644}; OrderedLocusNames=tsr1967;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-15, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
RA   Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y., Satoh K.,
RA   Sugiura M.;
RT   "Ycf12 is a core subunit in the photosystem II complex.";
RL   Biochim. Biophys. Acta 1767:1269-1275(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-10, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17967798; DOI=10.1093/pcp/pcm148;
RA   Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
RT   "Absence of the PsbZ subunit prevents association of PsbK and Ycf12 with
RT   the PSII complex in the thermophilic cyanobacterium Thermosynechococcus
RT   elongatus BP-1.";
RL   Plant Cell Physiol. 48:1758-1763(2007).
RN   [4] {ECO:0000312|PDB:1S5L}
RP   X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14764885; DOI=10.1126/science.1093087;
RA   Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
RT   "Architecture of the photosynthetic oxygen-evolving center.";
RL   Science 303:1831-1838(2004).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=16355230; DOI=10.1038/nature04224;
RA   Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
RT   "Towards complete cofactor arrangement in the 3.0 A resolution structure of
RT   photosystem II.";
RL   Nature 438:1040-1044(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS SPECTROMETRY, AND
RP   TOPOLOGY.
RC   STRAIN=BP-1;
RX   PubMed=19219048; DOI=10.1038/nsmb.1559;
RA   Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
RT   "Cyanobacterial photosystem II at 2.9-A resolution and the role of
RT   quinones, lipids, channels and chloride.";
RL   Nat. Struct. Mol. Biol. 16:334-342(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=BP-1;
RX   PubMed=20558739; DOI=10.1074/jbc.m110.127589;
RA   Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
RA   Zouni A.;
RT   "Crystal structure of monomeric photosystem II from Thermosynechococcus
RT   elongatus at 3.6 A resolution.";
RL   J. Biol. Chem. 285:26255-26262(2010).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=21367867; DOI=10.1074/jbc.m110.215970;
RA   Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J., Kern J.,
RA   Muh F., Dau H., Saenger W., Zouni A.;
RT   "Structural basis of cyanobacterial photosystem II inhibition by the
RT   herbicide terbutryn.";
RL   J. Biol. Chem. 286:15964-15972(2011).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=22665786; DOI=10.1073/pnas.1204598109;
RA   Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
RA   Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
RA   Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J., McQueen T.A.,
RA   DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A., Schafer D.W.,
RA   Seibert M.M., Sokaras D., Weng T.C., Zwart P.H., White W.E., Adams P.D.,
RA   Bogan M.J., Boutet S., Williams G.J., Messinger J., Sauter N.K., Zouni A.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Room temperature femtosecond X-ray diffraction of photosystem II
RT   microcrystals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=23413188; DOI=10.1126/science.1234273;
RA   Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
RA   Glockner C., Hellmich J., Laksmono H., Sierra R.G., Lassalle-Kaiser B.,
RA   Koroidov S., Lampe A., Han G., Gul S., Difiore D., Milathianaki D.,
RA   Fry A.R., Miahnahri A., Schafer D.W., Messerschmidt M., Seibert M.M.,
RA   Koglin J.E., Sokaras D., Weng T.C., Sellberg J., Latimer M.J.,
RA   Grosse-Kunstleve R.W., Zwart P.H., White W.E., Glatzel P., Adams P.D.,
RA   Bogan M.J., Williams G.J., Boutet S., Messinger J., Zouni A., Sauter N.K.,
RA   Yachandra V.K., Bergmann U., Yano J.;
RT   "Simultaneous femtosecond X-ray spectroscopy and diffraction of photosystem
RT   II at room temperature.";
RL   Science 340:491-495(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25043005; DOI=10.1038/nature13453;
RA   Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A., Rendek K.N.,
RA   Hunter M.S., Shoeman R.L., White T.A., Wang D., James D., Yang J.H.,
RA   Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A., Aquila A.L.,
RA   Deponte D., Kirian R.A., Bari S., Bergkamp J.J., Beyerlein K.R.,
RA   Bogan M.J., Caleman C., Chao T.C., Conrad C.E., Davis K.M.,
RA   Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S., Laksmono H.,
RA   Liang M., Lomb L., Marchesini S., Martin A.V., Messerschmidt M.,
RA   Milathianaki D., Nass K., Ros A., Roy-Chowdhury S., Schmidt K., Seibert M.,
RA   Steinbrener J., Stellato F., Yan L., Yoon C., Moore T.A., Moore A.L.,
RA   Pushkar Y., Williams G.J., Boutet S., Doak R.B., Weierstall U., Frank M.,
RA   Chapman H.N., Spence J.C., Fromme P.;
RT   "Serial time-resolved crystallography of photosystem II using a femtosecond
RT   X-ray laser.";
RL   Nature 513:261-265(2014).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
RP   COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BP-1;
RX   PubMed=25006873; DOI=10.1038/ncomms5371;
RA   Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
RA   Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
RA   Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S., Stan C.A.,
RA   Gloeckner C., Lampe A., DiFiore D., Milathianaki D., Fry A.R.,
RA   Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D., Weng T.C.,
RA   Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M., Glatzel P.,
RA   Williams G.J., Boutet S., Adams P.D., Zouni A., Messinger J., Sauter N.K.,
RA   Bergmann U., Yano J., Yachandra V.K.;
RT   "Taking snapshots of photosynthetic water oxidation using femtosecond X-ray
RT   diffraction and spectroscopy.";
RL   Nat. Commun. 5:4371-4371(2014).
CC   -!- FUNCTION: Controls the interaction of photosystem II (PSII) cores with
CC       the light-harvesting antenna. May also aid in binding of PsbK, Ycf12
CC       and the oxygen-evolving complex to PSII, at least in vitro. PSII is a
CC       light-driven water plastoquinone oxidoreductase, using light energy to
CC       abstract electrons from H(2)O, generating a proton gradient
CC       subsequently used for ATP formation. {ECO:0000255|HAMAP-Rule:MF_00644,
CC       ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:25006873}.
CC   -!- COFACTOR:
CC       Note=PSII binds multiple chlorophylls, carotenoids and specific lipids.
CC       {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005};
CC   -!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of membrane
CC       proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI, PsbJ, PsbK,
CC       PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3 peripheral proteins PsbO,
CC       PsbU, PsbV and a large number of cofactors. It forms dimeric complexes.
CC       {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}.
CC   -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00644, ECO:0000269|PubMed:14764885,
CC       ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
CC       ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:19219048,
CC       ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
CC       ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
CC       ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}; Multi-pass
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_00644,
CC       ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
CC       ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
CC       ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
CC       ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
CC       ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
CC       ECO:0000269|PubMed:25043005}. Note=Associated with the photosystem II
CC       complex.
CC   -!- MASS SPECTROMETRY: Mass=6798; Mass_error=5; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:19219048};
CC   -!- MASS SPECTROMETRY: Mass=6793; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20558739};
CC   -!- DISRUPTION PHENOTYPE: Cells grow normally under all light regimes
CC       tested; it is dispensable for photoautotrophic growth. The deletion
CC       strain is more tolerant to photoinhibition, while isolated PSII complex
CC       contains less PsbK and Ycf12 than wild-type and also has reduced
CC       oxygen-evolving capacity. {ECO:0000269|PubMed:17967798}.
CC   -!- SIMILARITY: Belongs to the PsbZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00644}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000039; BAC09519.1; -; Genomic_DNA.
DR   RefSeq; NP_682757.1; NC_004113.1.
DR   RefSeq; WP_011057802.1; NC_004113.1.
DR   PDB; 1S5L; X-ray; 3.50 A; Z/z=1-62.
DR   PDB; 2AXT; X-ray; 3.00 A; Z/z=1-62.
DR   PDB; 3KZI; X-ray; 3.60 A; Z=1-62.
DR   PDB; 4FBY; X-ray; 6.56 A; Z/l=1-62.
DR   PDB; 4IXQ; X-ray; 5.70 A; Z/z=1-62.
DR   PDB; 4IXR; X-ray; 5.90 A; Z/z=1-62.
DR   PDB; 4PBU; X-ray; 5.00 A; Z/z=1-62.
DR   PDB; 4PJ0; X-ray; 2.44 A; Z/z=1-62.
DR   PDB; 4RVY; X-ray; 5.50 A; Z/z=1-62.
DR   PDB; 4TNH; X-ray; 4.90 A; Z/z=1-62.
DR   PDB; 4TNI; X-ray; 4.60 A; Z/z=1-62.
DR   PDB; 4TNJ; X-ray; 4.50 A; Z/z=1-62.
DR   PDB; 4TNK; X-ray; 5.20 A; Z/z=1-62.
DR   PDB; 4V62; X-ray; 2.90 A; AZ/BZ=1-62.
DR   PDB; 4V82; X-ray; 3.20 A; AZ/BZ=1-62.
DR   PDB; 5E79; X-ray; 3.50 A; Z/z=1-62.
DR   PDB; 5E7C; X-ray; 4.50 A; Z/z=1-62.
DR   PDB; 5H2F; X-ray; 2.20 A; Z/z=1-62.
DR   PDB; 5KAF; X-ray; 3.00 A; Z/z=1-62.
DR   PDB; 5KAI; X-ray; 2.80 A; Z/z=1-62.
DR   PDB; 5MX2; X-ray; 2.20 A; Z/z=1-62.
DR   PDB; 5TIS; X-ray; 2.25 A; Z/z=1-62.
DR   PDB; 5ZZN; X-ray; 2.10 A; Z/z=1-62.
DR   PDB; 6DHE; X-ray; 2.05 A; Z/z=1-62.
DR   PDB; 6DHF; X-ray; 2.08 A; Z/z=1-62.
DR   PDB; 6DHG; X-ray; 2.50 A; Z/z=1-62.
DR   PDB; 6DHH; X-ray; 2.20 A; Z/z=1-62.
DR   PDB; 6DHO; X-ray; 2.07 A; Z/z=1-62.
DR   PDB; 6DHP; X-ray; 2.04 A; Z/z=1-62.
DR   PDB; 6W1O; X-ray; 2.08 A; Z/z=1-62.
DR   PDB; 6W1P; X-ray; 2.26 A; Z/z=1-62.
DR   PDB; 6W1Q; X-ray; 2.27 A; Z/z=1-62.
DR   PDB; 6W1R; X-ray; 2.23 A; Z/z=1-62.
DR   PDB; 6W1T; X-ray; 2.01 A; Z/z=1-62.
DR   PDB; 6W1U; X-ray; 2.09 A; Z/z=1-62.
DR   PDB; 6W1V; X-ray; 2.09 A; Z/z=1-62.
DR   PDBsum; 1S5L; -.
DR   PDBsum; 2AXT; -.
DR   PDBsum; 3KZI; -.
DR   PDBsum; 4FBY; -.
DR   PDBsum; 4IXQ; -.
DR   PDBsum; 4IXR; -.
DR   PDBsum; 4PBU; -.
DR   PDBsum; 4PJ0; -.
DR   PDBsum; 4RVY; -.
DR   PDBsum; 4TNH; -.
DR   PDBsum; 4TNI; -.
DR   PDBsum; 4TNJ; -.
DR   PDBsum; 4TNK; -.
DR   PDBsum; 4V62; -.
DR   PDBsum; 4V82; -.
DR   PDBsum; 5E79; -.
DR   PDBsum; 5E7C; -.
DR   PDBsum; 5H2F; -.
DR   PDBsum; 5KAF; -.
DR   PDBsum; 5KAI; -.
DR   PDBsum; 5MX2; -.
DR   PDBsum; 5TIS; -.
DR   PDBsum; 5ZZN; -.
DR   PDBsum; 6DHE; -.
DR   PDBsum; 6DHF; -.
DR   PDBsum; 6DHG; -.
DR   PDBsum; 6DHH; -.
DR   PDBsum; 6DHO; -.
DR   PDBsum; 6DHP; -.
DR   PDBsum; 6W1O; -.
DR   PDBsum; 6W1P; -.
DR   PDBsum; 6W1Q; -.
DR   PDBsum; 6W1R; -.
DR   PDBsum; 6W1T; -.
DR   PDBsum; 6W1U; -.
DR   PDBsum; 6W1V; -.
DR   SMR; Q8DHJ2; -.
DR   DIP; DIP-48504N; -.
DR   IntAct; Q8DHJ2; 1.
DR   STRING; 197221.22295693; -.
DR   EnsemblBacteria; BAC09519; BAC09519; BAC09519.
DR   KEGG; tel:tsr1967; -.
DR   PATRIC; fig|197221.4.peg.2057; -.
DR   eggNOG; ENOG5032ZB0; Bacteria.
DR   OMA; NWEQSKS; -.
DR   OrthoDB; 2012567at2; -.
DR   EvolutionaryTrace; Q8DHJ2; -.
DR   Proteomes; UP000000440; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
DR   GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0042549; P:photosystem II stabilization; IEA:InterPro.
DR   Gene3D; 1.10.287.740; -; 1.
DR   HAMAP; MF_00644; PSII_PsbZ; 1.
DR   InterPro; IPR002644; PSII_PsbZ.
DR   InterPro; IPR036512; PSII_PsbZ_sf.
DR   PANTHER; PTHR34971; PTHR34971; 1.
DR   Pfam; PF01737; Ycf9; 1.
DR   SUPFAM; SSF161055; SSF161055; 1.
DR   TIGRFAMs; TIGR03043; PS_II_psbZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Formylation; Membrane;
KW   Photosynthesis; Photosystem II; Reaction center; Reference proteome;
KW   Thylakoid; Transmembrane; Transmembrane helix.
FT   CHAIN           1..62
FT                   /note="Photosystem II reaction center protein Z"
FT                   /id="PRO_0000217733"
FT   TOPO_DOM        1..10
FT                   /note="Lumenal"
FT   TRANSMEM        11..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00644,
FT                   ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        25..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   TRANSMEM        39..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00644,
FT                   ECO:0000269|PubMed:19219048"
FT   TOPO_DOM        54..62
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:19219048"
FT   MOD_RES         1
FT                   /note="N-formylmethionine"
FT                   /evidence="ECO:0000269|PubMed:19219048,
FT                   ECO:0000269|PubMed:20558739"
FT   HELIX           4..27
FT                   /evidence="ECO:0007744|PDB:5ZZN"
FT   STRAND          29..31
FT                   /evidence="ECO:0007744|PDB:5MX2"
FT   HELIX           33..61
FT                   /evidence="ECO:0007744|PDB:5ZZN"
SQ   SEQUENCE   62 AA;  6764 MW;  313A629F73715DD8 CRC64;
     MTILFQLALA ALVILSFVMV IGVPVAYASP QDWDRSKQLI FLGSGLWIAL VLVVGVLNFF
     VV
//
DBGET integrated database retrieval system