Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Listeriolysin O (LLO) (Thiol-activated cytolysin)

 TACY_LISMO              Reviewed;         529 AA.
P13128; Q48747; Q57096; Q57206;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
22-NOV-2017, entry version 133.
RecName: Full=Listeriolysin O;
AltName: Full=LLO;
AltName: Full=Thiol-activated cytolysin;
Flags: Precursor;
Name=hly; Synonyms=hlyA, lisA; OrderedLocusNames=lmo0202;
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
NCBI_TaxID=169963;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=EGD / Serovar 1/2a;
PubMed=2505236; DOI=10.1093/nar/17.15.6406;
Domann E., Chakraborty T.;
"Nucleotide sequence of the listeriolysin gene from a Listeria
monocytogenes serotype 1/2a strain.";
Nucleic Acids Res. 17:6406-6406(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3126142;
Mengaud J., Vicente M.-F., Chenevert J., Pereira J.M., Geoffroy C.,
Gicquel-Sanzey B., Baquero F., Perez-Diaz J.-C., Cossart P.;
"Expression in Escherichia coli and sequence analysis of the
listeriolysin O determinant of Listeria monocytogenes.";
Infect. Immun. 56:766-772(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=12067;
PubMed=1937753;
Rasmussen O.F., Beck T., Olsen J.E., Dons L., Rossen L.;
"Listeria monocytogenes isolates can be classified into two major
types according to the sequence of the listeriolysin gene.";
Infect. Immun. 59:3945-3951(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=F4233 / Serotype 1/2b, F5782 / Serotype 4b, and
F6789 / Serotype 1/2b;
PubMed=9541569; DOI=10.1007/s002849900315;
Vines A., Swaminathan B.;
"Identification and characterization of nucleotide sequence
differences in three virulence-associated genes of Listeria
monocytogenes strains representing clinically important serotypes.";
Curr. Microbiol. 36:309-318(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-679 / EGD-e;
PubMed=11679669; DOI=10.1126/science.1063447;
Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
"Comparative genomics of Listeria species.";
Science 294:849-852(2001).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 413-480.
PubMed=2824384;
Mengaud J., Chenevert J., Geoffroy C., Gaillard J.-L., Cossart P.;
"Identification of the structural gene encoding the SH-activated
hemolysin of Listeria monocytogenes: listeriolysin O is homologous to
streptolysin O and pneumolysin.";
Infect. Immun. 55:3225-3227(1987).
[7]
FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBCELLULAR LOCATION.
STRAIN=EGD / Serovar 1/2a;
PubMed=3110067;
Geoffroy C., Gaillard J.L., Alouf J.E., Berche P.;
"Purification, characterization, and toxicity of the sulfhydryl-
activated hemolysin listeriolysin O from Listeria monocytogenes.";
Infect. Immun. 55:1641-1646(1987).
[8]
MUTAGENESIS OF CYS-484; TRP-491 AND TRP-492.
PubMed=1965218; DOI=10.1111/j.1365-2958.1990.tb00578.x;
Michel E., Reich K.A., Favier R., Berche P., Cossart P.;
"Attenuated mutants of the intracellular bacterium Listeria
monocytogenes obtained by single amino acid substitutions in
listeriolysin O.";
Mol. Microbiol. 4:2167-2178(1990).
[9]
FUNCTION, AND MUTAGENESIS OF CYS-484; TRP-491 AND TRP-492.
STRAIN=SLCC 5764 / Serovar 1/2a;
PubMed=8675352;
Tang P., Rosenshine I., Cossart P., Finlay B.B.;
"Listeriolysin O activates mitogen-activated protein kinase in
eucaryotic cells.";
Infect. Immun. 64:2359-2361(1996).
[10]
ENZYME REGULATION.
PubMed=9314564; DOI=10.1084/jem.186.7.1159;
Beauregard K.E., Lee K.D., Collier R.J., Swanson J.A.;
"pH-dependent perforation of macrophage phagosomes by listeriolysin O
from Listeria monocytogenes.";
J. Exp. Med. 186:1159-1163(1997).
[11]
DOMAIN.
STRAIN=EGD / Serovar 1/2a;
PubMed=11251831; DOI=10.1111/j.1365-2958.2001.02281.x;
Lety M.A., Frehel C., Dubail I., Beretti J.L., Kayal S., Berche P.,
Charbit A.;
"Identification of a PEST-like motif in listeriolysin O required for
phagosomal escape and for virulence in Listeria monocytogenes.";
Mol. Microbiol. 39:1124-1139(2001).
[12]
FUNCTION, REGULATION BY PH, AND MUTAGENESIS OF LEU-461.
STRAIN=10403S / Serovar 1/2a;
PubMed=11901168; DOI=10.1083/jcb.200201081;
Glomski I.J., Gedde M.M., Tsang A.W., Swanson J.A., Portnoy D.A.;
"The Listeria monocytogenes hemolysin has an acidic pH optimum to
compartmentalize activity and prevent damage to infected host cells.";
J. Cell Biol. 156:1029-1038(2002).
[13]
DOMAIN, AND MUTAGENESIS OF PRO-49; LYS-50 AND PRO-52.
STRAIN=EGD / Serovar 1/2a;
PubMed=12406215; DOI=10.1046/j.1365-2958.2002.03176.x;
Lety M.A., Frehel C., Berche P., Charbit A.;
"Critical role of the N-terminal residues of listeriolysin O in
phagosomal escape and virulence of Listeria monocytogenes.";
Mol. Microbiol. 46:367-379(2002).
[14]
PHOSPHORYLATION, UBIQUITINATION, DOMAIN, ENZYME REGULATION, AND
MUTAGENESIS OF SER-44.
STRAIN=10403S / Serovar 1/2a;
PubMed=16441444; DOI=10.1111/j.1462-5822.2005.00631.x;
Schnupf P., Portnoy D.A., Decatur A.L.;
"Phosphorylation, ubiquitination and degradation of listeriolysin O in
mammalian cells: role of the PEST-like sequence.";
Cell. Microbiol. 8:353-364(2006).
[15]
ENZYME REGULATION.
STRAIN=10403S / Serovar 1/2a;
PubMed=16859495; DOI=10.1111/j.1365-2958.2006.05286.x;
Schnupf P., Hofmann J., Norseen J., Glomski I.J., Schwartzstein H.,
Decatur A.L.;
"Regulated translation of listeriolysin O controls virulence of
Listeria monocytogenes.";
Mol. Microbiol. 61:999-1012(2006).
[16]
REVIEW.
PubMed=17720603; DOI=10.1016/j.micinf.2007.05.005;
Schnupf P., Portnoy D.A.;
"Listeriolysin O: a phagosome-specific lysin.";
Microbes Infect. 9:1176-1187(2007).
[17]
FUNCTION IN SLAPS FORMATION.
STRAIN=10403S / Serovar 1/2a;
PubMed=18202661; DOI=10.1038/nature06479;
Birmingham C.L., Canadien V., Kaniuk N.A., Steinberg B.E.,
Higgins D.E., Brumell J.H.;
"Listeriolysin O allows Listeria monocytogenes replication in
macrophage vacuoles.";
Nature 451:350-354(2008).
[18]
FUNCTION.
STRAIN=EGD / Serovar 1/2a;
PubMed=20414307; DOI=10.1038/nature08963;
Ribet D., Hamon M., Gouin E., Nahori M.A., Impens F., Neyret-Kahn H.,
Gevaert K., Vandekerckhove J., Dejean A., Cossart P.;
"Listeria monocytogenes impairs SUMOylation for efficient infection.";
Nature 464:1192-1195(2010).
-!- FUNCTION: Sulfhydryl-activated pore-forming toxin, which is a
major virulence factor required for the escape of bacteria from
phagosomal vacuoles and entry into the host cytosol. After binding
to target membranes, the protein undergoes a major conformation
change, leading to its insertion in the host membrane and
formation of an oligomeric pore complex. Listeriolysin O activates
mitogen-activated protein (MAP) kinase activity in host cells,
most likely as a result of the permeabilization of the host cell
membrane. Also induces a proteasome-independent degradation of
UBE2I (the SUMO-conjugating enzyme UBC9) and a proteasome-
dependent degradation of some sumoylated proteins. Finally, is
necessary and sufficient for spacious Listeria-containing
phagosomes (SLAPs) formation, suggesting a role for listeriolysin
O in promoting L.monocytogenes replication in vacuoles, leading to
persistent infection. {ECO:0000269|PubMed:11901168,
ECO:0000269|PubMed:18202661, ECO:0000269|PubMed:20414307,
ECO:0000269|PubMed:3110067, ECO:0000269|PubMed:8675352}.
-!- ENZYME REGULATION: Activity of listeriolysin O is regulated on
multiple levels. It should be high in the phagosome, thereby
allowing escape of the bacteria from the phagosomal compartment.
Then, once inside the host cytosol, the activity must be
controlled to prevent lysis of the host plasma membrane and loss
of the intracellular environment. Multiple regulatory mechanisms
include translational repression, which is required to minimize
levels of listeriolysin O in the host cytosol. In addition,
cytolytic activity is pH-dependent. Activity is high in the acidic
environment of the phagosome and is turned off in the neutral pH
of the cytosol. Listeriolysin O is also ubiquitinated and rapidly
degraded by host proteasome in cytosol. The lytic activity is
activated by reducing agents and suppressed by oxidation. Also
inhibited by very low amounts of cholesterol.
{ECO:0000269|PubMed:16441444, ECO:0000269|PubMed:16859495,
ECO:0000269|PubMed:3110067, ECO:0000269|PubMed:9314564}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5. Cytolytic activity is undetectable at pH 7.0.
{ECO:0000269|PubMed:3110067};
-!- SUBUNIT: Homooligomeric pore complex; when inserted in the host
membrane.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-6407357, EBI-6407357;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3110067}. Host
membrane {ECO:0000269|PubMed:3110067}; Multi-pass membrane protein
{ECO:0000269|PubMed:3110067}. Host cell membrane
{ECO:0000269|PubMed:3110067}; Multi-pass membrane protein
{ECO:0000269|PubMed:3110067}. Note=Secreted as soluble protein
that then inserts into the host membrane and forms pores formed by
transmembrane beta-strands. {ECO:0000250}.
-!- DOMAIN: The N-terminal region is not required for secretion and
hemolytic activity, but is involved in phagosomal escape of
bacteria in infected cells and is critical for bacterial
virulence. This region contains a PEST-like sequence, which does
not mediate proteasomal degradation, but controls listeriolysin O
production in the cytosol. {ECO:0000269|PubMed:11251831,
ECO:0000269|PubMed:12406215, ECO:0000269|PubMed:16441444}.
-!- PTM: Phosphorylated. Phosphorylation does not appear to be
required for ubiquitination or degradation.
{ECO:0000269|PubMed:16441444}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:16441444}.
-!- SIMILARITY: Belongs to the thiol-activated cytolysin family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA69528.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAA69531.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X15127; CAA33223.1; -; Genomic_DNA.
EMBL; M24199; AAA03018.1; -; Unassigned_DNA.
EMBL; X60035; CAA42639.1; -; Genomic_DNA.
EMBL; U25446; AAA69528.1; ALT_INIT; Genomic_DNA.
EMBL; U25449; AAA69531.1; ALT_INIT; Genomic_DNA.
EMBL; U25452; AAA69534.1; -; Genomic_DNA.
EMBL; AL591974; CAD00729.1; -; Genomic_DNA.
PIR; A43505; A43505.
PIR; AC1100; AC1100.
PIR; S24231; S24231.
RefSeq; NP_463733.1; NC_003210.1.
RefSeq; WP_003722731.1; NC_003210.1.
PDB; 4CDB; X-ray; 2.15 A; A=39-526.
PDBsum; 4CDB; -.
ProteinModelPortal; P13128; -.
SMR; P13128; -.
IntAct; P13128; 1.
MINT; MINT-8216036; -.
STRING; 169963.lmo0202; -.
TCDB; 1.C.12.1.7; the thiol-activated cholesterol-dependent cytolysin (cdc) family.
iPTMnet; P13128; -.
PaxDb; P13128; -.
PRIDE; P13128; -.
EnsemblBacteria; CAD00729; CAD00729; CAD00729.
GeneID; 987033; -.
KEGG; lmo:lmo0202; -.
PATRIC; fig|169963.11.peg.207; -.
eggNOG; ENOG4105E5P; Bacteria.
eggNOG; ENOG410XQPX; LUCA.
KO; K11031; -.
OMA; NDRTYPG; -.
Proteomes; UP000000817; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0015485; F:cholesterol binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; IEA:UniProtKB-KW.
Gene3D; 3.90.840.10; -; 2.
InterPro; IPR035390; Thiol_cytolys_C.
InterPro; IPR001869; Thiol_cytolysin.
InterPro; IPR036363; Thiol_cytolysin_ab_sf.
InterPro; IPR036359; Thiol_cytolysin_sf.
Pfam; PF17440; Thiol_cytolys_C; 1.
Pfam; PF01289; Thiol_cytolysin; 1.
PRINTS; PR01400; TACYTOLYSIN.
SUPFAM; SSF56978; SSF56978; 1.
PROSITE; PS00481; THIOL_CYTOLYSINS; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytolysis; Hemolysis;
Host cell membrane; Host membrane; Lipid-binding; Membrane;
Phosphoprotein; Reference proteome; Secreted; Signal; Toxin;
Transmembrane; Transmembrane beta strand; Ubl conjugation; Virulence.
SIGNAL 1 25
CHAIN 26 529 Listeriolysin O.
/FTId=PRO_0000034102.
SITE 484 484 Binding to cholesterol. {ECO:0000250}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000305|PubMed:16441444}.
VARIANT 35 35 S -> L (in strain: F4233 / Serotype 1/2b,
F5782 / Serotype 4b, F6789 / Serotype 1/
2b and 12067).
VARIANT 438 438 V -> I (in strain: F4233 / Serotype 1/2b,
F5782 / Serotype 4b, F6789 / Serotype 1/
2b and 12067).
VARIANT 523 523 K -> S (in strain: F4233 / Serotype 1/2b,
F5782 / Serotype 4b, F6789 / Serotype 1/
2b and 12067).
MUTAGEN 44 44 S->A: 1500-fold decrease in virulence.
{ECO:0000269|PubMed:16441444}.
MUTAGEN 49 49 P->A: Does not affect secretion and
hemolytic activity. No defect in
phagosomal escape. Shows a clear
attenuation in virulence.
{ECO:0000269|PubMed:12406215}.
MUTAGEN 50 50 K->A: Does not affect secretion and
hemolytic activity. Slight decrease in
phagosomal escape. Shows a clear
attenuation in virulence.
{ECO:0000269|PubMed:12406215}.
MUTAGEN 52 52 P->A: Does not affect secretion and
hemolytic activity. Slight decrease in
phagosomal escape. Shows a clear
attenuation in virulence.
{ECO:0000269|PubMed:12406215}.
MUTAGEN 461 461 L->T: 10-fold increase in hemolytic
activity at neutral pH, but 100-fold
decrease in virulence.
{ECO:0000269|PubMed:11901168}.
MUTAGEN 484 484 C->A: 25% decrease in hemolytic activity,
but still able to stimulate MAP kinase
tyrosine phosphorylation in host cells.
Does not affect membrane-binding
capacity. {ECO:0000269|PubMed:1965218,
ECO:0000269|PubMed:8675352}.
MUTAGEN 484 484 C->S: 80% decrease in hemolytic activity,
but still able to stimulate MAP kinase
tyrosine phosphorylation in host cells.
Does not affect membrane-binding
capacity. {ECO:0000269|PubMed:1965218,
ECO:0000269|PubMed:8675352}.
MUTAGEN 491 491 W->A: 95% decrease in hemolytic activity
and no stimulation of MAP kinase
activity. Does not affect membrane-
binding capacity.
{ECO:0000269|PubMed:1965218,
ECO:0000269|PubMed:8675352}.
MUTAGEN 492 492 W->A: 99.9% decrease in hemolytic
activity and no stimulation of MAP kinase
activity. Does not affect membrane-
binding capacity.
{ECO:0000269|PubMed:1965218,
ECO:0000269|PubMed:8675352}.
SEQUENCE 529 AA; 58688 MW; 83B6B0C11C033FB1 CRC64;
MKKIMLVFIT LILVSLPIAQ QTEAKDASAF NKENSISSMA PPASPPASPK TPIEKKHADE
IDKYIQGLDY NKNNVLVYHG DAVTNVPPRK GYKDGNEYIV VEKKKKSINQ NNADIQVVNA
ISSLTYPGAL VKANSELVEN QPDVLPVKRD SLTLSIDLPG MTNQDNKIVV KNATKSNVNN
AVNTLVERWN EKYAQAYPNV SAKIDYDDEM AYSESQLIAK FGTAFKAVNN SLNVNFGAIS
EGKMQEEVIS FKQIYYNVNV NEPTRPSRFF GKAVTKEQLQ ALGVNAENPP AYISSVAYGR
QVYLKLSTNS HSTKVKAAFD AAVSGKSVSG DVELTNIIKN SSFKAVIYGG SAKDEVQIID
GNLGDLRDIL KKGATFNRET PGVPIAYTTN FLKDNELAVI KNNSEYIETT SKAYTDGKIN
IDHSGGYVAQ FNISWDEVNY DPEGNEIVQH KNWSENNKSK LAHFTSSIYL PGNARNINVY
AKECTGLAWE WWRTVIDDRN LPLVKNRNIS IWGTTLYPKY SNKVDNPIE


Related products :

Catalog number Product name Quantity
10-663-45609 Listeriolysin-O (LLO) - Thiol-activated cytolysin; LLO N_A 0.1 mg
10-663-45609 Listeriolysin-O (LLO) - Thiol-activated cytolysin; LLO N_A 0.05 mg
10-663-45609 Listeriolysin-O (LLO) - Thiol-activated cytolysin; LLO N_A 0.01 mg
orb81199 Listeriolysin-O protein Molecular weight of Listeriolysin is 58kDa. This haemolysin protein is provided in its mature form that is constituted by 503 amino acids, from 26 to 529 of the registered sequ 10
S-9116.0100 Fluoro Thiol™ _ Fluorescent Thiol Detection Kit 100T
orb81200 Listeriolysin-O PEST-free protein Recombinant Listeriolysin lacking both the signal secretion sequence and the PEST- like sequence. LLO-PEST minus is composed of 471 amino acids, starting from amino a 10
K3005-1 Thiol Fluorescent Detection Kit Free thiols in biological systems have important roles. Oxidatively modified thiol groups of cysteine residues are known to modulate the activity of a growing number of 96 rxns
gen16946 PERF_RAT Cytolysin ELISA tesk kit 1
gen16940 PERF_MOUSE Cytolysin ELISA tesk kit 1
gen16933 PERF_HUMAN Cytolysin ELISA tesk kit 1
OBT1635 Perforin, Cytolysin, 70kD, Clone dG9, Mab anti_Human; frozen, IH_flow_IP 50 µg.
E1317r ELISA Cytolysin,Lymphocyte pore-forming protein,P1,Perforin-1,Pfp,Prf1,Rat,Rattus norvegicus 96T
H-1106.0500 Stoichactis helianthus Cytolysin (non_synthetic) Salt _ Binding _ Synonym SumFormula C766H1173N201O224S6 0.5 mg
E1317m ELISA Cytolysin,Lymphocyte pore-forming protein,Mouse,Mus musculus,P1,Perforin-1,Pfp,Prf1 96T
E1317m ELISA kit Cytolysin,Lymphocyte pore-forming protein,Mouse,Mus musculus,P1,Perforin-1,Pfp,Prf1 96T
E1317r ELISA kit Cytolysin,Lymphocyte pore-forming protein,P1,Perforin-1,Pfp,Prf1,Rat,Rattus norvegicus 96T
U1317r CLIA Cytolysin,Lymphocyte pore-forming protein,P1,Perforin-1,Pfp,Prf1,Rat,Rattus norvegicus 96T
H-1106.1000 Stoichactis helianthus Cytolysin (non_synthetic) Salt _ Binding _ Synonym SumFormula C766H1173N201O224S6 1.0 mg
U1317m CLIA Cytolysin,Lymphocyte pore-forming protein,Mouse,Mus musculus,P1,Perforin-1,Pfp,Prf1 96T
E1317h ELISA kit Cytolysin,Homo sapiens,Human,Lymphocyte pore-forming protein,P1,Perforin-1,PFP,PFP,PRF1 96T
E1317h ELISA Cytolysin,Homo sapiens,Human,Lymphocyte pore-forming protein,P1,Perforin-1,PFP,PFP,PRF1 96T
U1317h CLIA Cytolysin,Homo sapiens,Human,Lymphocyte pore-forming protein,P1,Perforin-1,PFP,PFP,PRF1 96T
PG2-TH-2k Thiol PEG Thiol, HS-PEG-HS, 2000 Da 1 g
PG2-TH-5k Thiol PEG Thiol, HS-PEG-HS, 5000 Da 1 g
PG2-TH-20k Thiol PEG Thiol, HS-PEG-HS, 20000 Da 1 g


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur