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Photosystem II reaction center protein T (PSII-T) (PSII-Tc)

 PSBT_THEEB              Reviewed;          32 AA.
Q8DIQ0; Q9F1M2;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-APR-2018, entry version 93.
RecName: Full=Photosystem II reaction center protein T {ECO:0000255|HAMAP-Rule:MF_00808};
Short=PSII-T {ECO:0000255|HAMAP-Rule:MF_00808};
Short=PSII-Tc {ECO:0000303|PubMed:15653799};
Name=psbT {ECO:0000255|HAMAP-Rule:MF_00808};
OrderedLocusNames=tsr1531;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15653799; DOI=10.1093/pcp/pch207;
Iwai M., Katoh H., Katayama M., Ikeuchi M.;
"PSII-Tc protein plays an important role in dimerization of
photosystem II.";
Plant Cell Physiol. 45:1809-1816(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[3]
PROTEIN SEQUENCE OF 1-15, COFACTOR, AND SUBCELLULAR LOCATION.
PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y.,
Satoh K., Sugiura M.;
"Ycf12 is a core subunit in the photosystem II complex.";
Biochim. Biophys. Acta 1767:1269-1275(2007).
[4]
PROTEIN SEQUENCE OF 1-9, COFACTOR, AND SUBCELLULAR LOCATION.
PubMed=17967798; DOI=10.1093/pcp/pcm148;
Iwai M., Suzuki T., Dohmae N., Inoue Y., Ikeuchi M.;
"Absence of the PsbZ subunit prevents association of PsbK and Ycf12
with the PSII complex in the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
Plant Cell Physiol. 48:1758-1763(2007).
[5]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=14764885; DOI=10.1126/science.1093087;
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
"Architecture of the photosynthetic oxygen-evolving center.";
Science 303:1831-1838(2004).
[6]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=16355230; DOI=10.1038/nature04224;
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
"Towards complete cofactor arrangement in the 3.0 A resolution
structure of photosystem II.";
Nature 438:1040-1044(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, MASS
SPECTROMETRY, AND TOPOLOGY.
STRAIN=BP-1;
PubMed=19219048; DOI=10.1038/nsmb.1559;
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
"Cyanobacterial photosystem II at 2.9-A resolution and the role of
quinones, lipids, channels and chloride.";
Nat. Struct. Mol. Biol. 16:334-342(2009).
[8]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, FORMYLATION AT MET-1, AND
MASS SPECTROMETRY.
STRAIN=BP-1;
PubMed=20558739; DOI=10.1074/jbc.M110.127589;
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
Zouni A.;
"Crystal structure of monomeric photosystem II from
Thermosynechococcus elongatus at 3.6 A resolution.";
J. Biol. Chem. 285:26255-26262(2010).
[9]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=21367867; DOI=10.1074/jbc.M110.215970;
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J.,
Kern J., Muh F., Dau H., Saenger W., Zouni A.;
"Structural basis of cyanobacterial photosystem II inhibition by the
herbicide terbutryn.";
J. Biol. Chem. 286:15964-15972(2011).
[10]
X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=22665786; DOI=10.1073/pnas.1204598109;
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J.,
McQueen T.A., DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A.,
Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H.,
White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J.,
Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J.,
Yachandra V.K.;
"Room temperature femtosecond X-ray diffraction of photosystem II
microcrystals.";
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
[11]
X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=23413188; DOI=10.1126/science.1234273;
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
Glockner C., Hellmich J., Laksmono H., Sierra R.G.,
Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D.,
Milathianaki D., Fry A.R., Miahnahri A., Schafer D.W.,
Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C.,
Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H.,
White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J.,
Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K.,
Bergmann U., Yano J.;
"Simultaneous femtosecond X-ray spectroscopy and diffraction of
photosystem II at room temperature.";
Science 340:491-495(2013).
[12]
X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 1-30 IN PHOTOSYSTEM II,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25043005; DOI=10.1038/nature13453;
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A.,
Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D.,
Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A.,
Aquila A.L., Deponte D., Kirian R.A., Bari S., Bergkamp J.J.,
Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E.,
Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S.,
Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V.,
Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S.,
Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C.,
Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S.,
Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C.,
Fromme P.;
"Serial time-resolved crystallography of photosystem II using a
femtosecond X-ray laser.";
Nature 513:261-265(2014).
[13]
X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25006873; DOI=10.1038/ncomms5371;
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S.,
Stan C.A., Gloeckner C., Lampe A., DiFiore D., Milathianaki D.,
Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D.,
Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M.,
Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A.,
Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.;
"Taking snapshots of photosynthetic water oxidation using femtosecond
X-ray diffraction and spectroscopy.";
Nat. Commun. 5:4371-4371(2014).
-!- FUNCTION: Seems to play a role in the dimerization of PSII. PSII
is a light-driven water plastoquinone oxidoreductase, using light
energy to abstract electrons from H(2)O, generating a proton
gradient subsequently used for ATP formation. {ECO:0000255|HAMAP-
Rule:MF_00808, ECO:0000269|PubMed:15653799,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:25006873}.
-!- COFACTOR:
Note=PSII binds multiple chlorophylls, carotenoids and specific
lipids. {ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005};
-!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of
membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI,
PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, 3
peripheral proteins PsbO, PsbU, PsbV and a large number of
cofactors. It forms dimeric complexes.
{ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_00808, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
ECO:0000269|PubMed:17967798, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005}; Single-
pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00808,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, ECO:0000269|PubMed:17967798,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:21367867, ECO:0000269|PubMed:22665786,
ECO:0000269|PubMed:23413188, ECO:0000269|PubMed:25006873,
ECO:0000269|PubMed:25043005}.
-!- MASS SPECTROMETRY: Mass=3906; Mass_error=4; Method=MALDI; Range=1-
32; Evidence={ECO:0000269|PubMed:19219048};
-!- MASS SPECTROMETRY: Mass=3904; Method=MALDI; Range=1-32;
Evidence={ECO:0000269|PubMed:20558739};
-!- DISRUPTION PHENOTYPE: No detectable dimeric PSII, loss of another
protein that may be PsbM. {ECO:0000269|PubMed:15653799}.
-!- SIMILARITY: Belongs to the PsbT family. {ECO:0000255|HAMAP-
Rule:MF_00808}.
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EMBL; AB052566; BAB19262.1; -; Genomic_DNA.
EMBL; BA000039; BAC09083.1; -; Genomic_DNA.
RefSeq; NP_682321.1; NC_004113.1.
RefSeq; WP_011057371.1; NC_004113.1.
PDB; 1S5L; X-ray; 3.50 A; T/t=1-32.
PDB; 2AXT; X-ray; 3.00 A; T/t=1-32.
PDB; 3KZI; X-ray; 3.60 A; T=1-32.
PDB; 4FBY; X-ray; 6.56 A; T/g=1-32.
PDB; 4IXQ; X-ray; 5.70 A; T/t=1-32.
PDB; 4IXR; X-ray; 5.90 A; T/t=1-32.
PDB; 4PBU; X-ray; 5.00 A; T/t=1-30.
PDB; 4PJ0; X-ray; 2.44 A; T/t=1-32.
PDB; 4RVY; X-ray; 5.50 A; T/t=1-30.
PDB; 4TNH; X-ray; 4.90 A; T/t=1-32.
PDB; 4TNI; X-ray; 4.60 A; T/t=1-32.
PDB; 4TNJ; X-ray; 4.50 A; T/t=1-32.
PDB; 4TNK; X-ray; 5.20 A; T/t=1-32.
PDB; 4V62; X-ray; 2.90 A; AT/BT=1-32.
PDB; 4V82; X-ray; 3.20 A; AT/BT=1-32.
PDB; 5E79; X-ray; 3.50 A; T/t=1-30.
PDB; 5E7C; X-ray; 4.50 A; T/t=1-30.
PDB; 5H2F; X-ray; 2.20 A; T/t=1-30.
PDB; 5KAF; X-ray; 3.00 A; T/t=2-32.
PDB; 5KAI; X-ray; 2.80 A; T/t=2-32.
PDB; 5MX2; X-ray; 2.20 A; T/t=1-32.
PDB; 5TIS; X-ray; 2.25 A; T/t=1-32.
PDBsum; 1S5L; -.
PDBsum; 2AXT; -.
PDBsum; 3KZI; -.
PDBsum; 4FBY; -.
PDBsum; 4IXQ; -.
PDBsum; 4IXR; -.
PDBsum; 4PBU; -.
PDBsum; 4PJ0; -.
PDBsum; 4RVY; -.
PDBsum; 4TNH; -.
PDBsum; 4TNI; -.
PDBsum; 4TNJ; -.
PDBsum; 4TNK; -.
PDBsum; 4V62; -.
PDBsum; 4V82; -.
PDBsum; 5E79; -.
PDBsum; 5E7C; -.
PDBsum; 5H2F; -.
PDBsum; 5KAF; -.
PDBsum; 5KAI; -.
PDBsum; 5MX2; -.
PDBsum; 5TIS; -.
ProteinModelPortal; Q8DIQ0; -.
SMR; Q8DIQ0; -.
DIP; DIP-48500N; -.
IntAct; Q8DIQ0; 1.
STRING; 197221.tsr1531; -.
EnsemblBacteria; BAC09083; BAC09083; BAC09083.
GeneID; 1011082; -.
KEGG; tel:tsr1531; -.
KO; K02718; -.
BioCyc; TELO197221:G1G3I-1557-MONOMER; -.
EvolutionaryTrace; Q8DIQ0; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
HAMAP; MF_00808; PSII_PsbT; 1.
InterPro; IPR001743; PSII_PsbT.
InterPro; IPR037268; PSII_PsbT_sf.
Pfam; PF01405; PsbT; 1.
SUPFAM; SSF161029; SSF161029; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Formylation; Membrane; Photosynthesis; Photosystem II;
Reference proteome; Thylakoid; Transmembrane; Transmembrane helix.
CHAIN 1 32 Photosystem II reaction center protein T.
/FTId=PRO_0000218004.
TOPO_DOM 1 3 Lumenal. {ECO:0000269|PubMed:19219048}.
TRANSMEM 4 18 Helical. {ECO:0000255|HAMAP-
Rule:MF_00808,
ECO:0000269|PubMed:19219048}.
TOPO_DOM 19 32 Cytoplasmic.
{ECO:0000269|PubMed:19219048}.
MOD_RES 1 1 N-formylmethionine.
{ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739}.
HELIX 2 22 {ECO:0000244|PDB:5MX2}.
SEQUENCE 32 AA; 3875 MW; D8557803A0A3C7E4 CRC64;
METITYVFIF ACIIALFFFA IFFREPPRIT KK


Related products :

Catalog number Product name Quantity
AS05059 PsbR | 10 kDa protein of PSII 100 ul
AS06 146 PsbD | D2 protein of PSII 100 ul
AS06146 PsbD | D2 protein of PSII 100 µl
20312122-1 PsbD- D2 protein of PSII 100 uL
20312152-1 PsbS | 22 kDa Lhc-like PSII protein (hen 100 uL
AS06146 PsbD | D2 protein of PSII 100 ul
AS06171 PsbTn | Tn protein of PSII
20312372-1 PsbS | 22 kDa Lhc-like PSII protein (rab 200 uL
AS05 059 PsbR | 10 kDa protein of PSII 100 ul
20312132-1 Hen PsbA - D1 protein of PSII, C-termina 10 uL
20312132-2 Hen PsbA - D1 protein of PSII, C-termina 100 uL
AS05084-10 PsbA | D1 protein of PSII, C_terminal (10 ul) 10 ul
AS09 533 PsbS | 22 kDa Lhc_like PSII protein 200 ul
20312123-1 PsbB- CP47 protein of PSII 50 uL
20312165-1 PsbR | 10 kDa protein of PSII (rabbit) 100 uL
AS06110 PsbC | CP43 protein of PSII 150 ul
AS03 032 hen polyclonal PsbS | 22 kDa Lhc-like PSII protein 100
AS01016-10 PsbA | D1 protein of PSII, C_terminal (10 ul) 10 ul
AS06115 PsbZ | ycf9 protein of PSII 200 ul
AS01016 PsbA | D1 protein of PSII, C_terminal 100 ul
AS06124A PsbA | D1 protein of PSII, N_terminal 200 ug
20312472-1 PsbA | D1 protein of PSII, N-terminal (r 200 uL
AS03032 PsbS | 22 kDa Lhc_like PSII protein 100 ul
AS04038 PsbB | CP47 protein of PSII 50 ul
AS01 016-10 PsbA | D1 protein of PSII, C_terminal (10 ul) 10 ul


 

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