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

Virulence sensor protein BvgS (EC 2.7.13.3)

 BVGS_BORPE              Reviewed;        1238 AA.
P16575; P16576;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 3.
28-FEB-2018, entry version 162.
RecName: Full=Virulence sensor protein BvgS;
EC=2.7.13.3;
Flags: Precursor;
Name=bvgS; OrderedLocusNames=BP1877;
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257313;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2549542; DOI=10.1073/pnas.86.17.6671;
Arico B., Miller J.F., Roy C., Stibitz S., Monack D.M., Falkow S.,
Gross R., Rappuoli R.;
"Sequences required for expression of Bordetella pertussis virulence
factors share homology with prokaryotic signal transduction
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 86:6671-6675(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
PubMed=1791760; DOI=10.1111/j.1365-2958.1991.tb02093.x;
Arico B., Scarlato V., Monack D.M., Falkow S., Rappuoli R.;
"Structural and genetic analysis of the bvg locus in Bordetella
species.";
Mol. Microbiol. 5:2481-2491(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
PubMed=12910271; DOI=10.1038/ng1227;
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 827-1153.
PubMed=2537932; DOI=10.1038/338266a0;
Stibitz S., Aaronson W., Monack D., Falkow S.;
"Phase variation in Bordetella pertussis by frameshift mutation in a
gene for a novel two-component system.";
Nature 338:266-269(1989).
[5]
MUTAGENESIS OF HIS-729 AND ASP-1023.
PubMed=8302847; DOI=10.1073/pnas.91.3.1163;
Uhl M.A., Miller J.F.;
"Autophosphorylation and phosphotransfer in the Bordetella pertussis
BvgAS signal transduction cascade.";
Proc. Natl. Acad. Sci. U.S.A. 91:1163-1167(1994).
[6]
MUTAGENESIS OF ASP-979; ASP-980; ASP-1023; LYS-1080; ARG-1146 AND
THR-1147.
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
PubMed=7752227; DOI=10.1006/jmbi.1995.0245;
Beier D., Schwarz B., Fuchs T.M., Gross R.;
"In vivo characterization of the unorthodox BvgS two-component sensor
protein of Bordetella pertussis.";
J. Mol. Biol. 248:596-610(1995).
[7]
CHARACTERIZATION, AND MUTAGENESIS OF HIS-1172.
PubMed=8605872;
Uhl M.A., Miller J.F.;
"Integration of multiple domains in a two-component sensor protein:
the Bordetella pertussis BvgAS phosphorelay.";
EMBO J. 15:1028-1036(1996).
[8]
CHARACTERIZATION.
PubMed=9535079; DOI=10.1046/j.1365-2958.1998.00716.x;
Perraud A.-L., Kimmel B., Weiss V., Gross R.;
"Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-
terminal HPt domains of the sensor proteins.";
Mol. Microbiol. 27:875-887(1998).
-!- FUNCTION: Member of the two-component regulatory system BvgS/BvgA.
Phosphorylates BvgA via a four-step phosphorelay in response to
environmental signals.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-
pass membrane protein {ECO:0000305}.
-!- PTM: Activation requires a sequential transfer of a phosphate
group from a His in the primary transmitter domain, to an Asp in
the receiver domain and to a His in the secondary transmitter
domain.
-!- CAUTION: Was originally thought to be two separate ORFs named bvgB
and bvgC. {ECO:0000305|PubMed:2549542}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M25401; AAA22970.1; -; Genomic_DNA.
EMBL; BX640416; CAE42160.1; -; Genomic_DNA.
PIR; A40185; A40185.
RefSeq; NP_880569.1; NC_002929.2.
RefSeq; WP_010930608.1; NC_002929.2.
PDB; 3MPK; X-ray; 2.04 A; A=287-542.
PDB; 3MPL; X-ray; 2.10 A; A=287-542.
PDB; 4Q0C; X-ray; 3.10 A; A/B/C/D=30-544.
PDBsum; 3MPK; -.
PDBsum; 3MPL; -.
PDBsum; 4Q0C; -.
ProteinModelPortal; P16575; -.
SMR; P16575; -.
STRING; 257313.BP1877; -.
PRIDE; P16575; -.
EnsemblBacteria; CAE42160; CAE42160; BP1877.
GeneID; 2667057; -.
KEGG; bpe:BP1877; -.
PATRIC; fig|257313.5.peg.2016; -.
eggNOG; ENOG4105BZU; Bacteria.
eggNOG; ENOG410XNMH; LUCA.
HOGENOM; HOG000269369; -.
KO; K07679; -.
OMA; HWILPYR; -.
BioCyc; BPER257313:G1GSZ-2220-MONOMER; -.
BRENDA; 2.7.13.3; 899.
EvolutionaryTrace; P16575; -.
Proteomes; UP000002676; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
CDD; cd00075; HATPase_c; 1.
CDD; cd00082; HisKA; 1.
CDD; cd00088; HPT; 1.
CDD; cd00130; PAS; 1.
CDD; cd00156; REC; 1.
Gene3D; 1.20.120.160; -; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR011006; CheY-like_superfamily.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR036097; HisK_dim/P_sf.
InterPro; IPR036641; HPT_dom_sf.
InterPro; IPR000014; PAS.
InterPro; IPR000700; PAS-assoc_C.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013767; PAS_fold.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
InterPro; IPR001638; Solute-binding_3/MltF_N.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00512; HisKA; 1.
Pfam; PF01627; Hpt; 1.
Pfam; PF00989; PAS; 1.
Pfam; PF00072; Response_reg; 1.
Pfam; PF00497; SBP_bac_3; 2.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00387; HATPase_c; 1.
SMART; SM00388; HisKA; 1.
SMART; SM00073; HPT; 1.
SMART; SM00091; PAS; 1.
SMART; SM00062; PBPb; 2.
SMART; SM00448; REC; 1.
SUPFAM; SSF47226; SSF47226; 2.
SUPFAM; SSF47384; SSF47384; 1.
SUPFAM; SSF52172; SSF52172; 1.
SUPFAM; SSF55785; SSF55785; 1.
SUPFAM; SSF55874; SSF55874; 1.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50109; HIS_KIN; 1.
PROSITE; PS50894; HPT; 1.
PROSITE; PS50113; PAC; 1.
PROSITE; PS50112; PAS; 1.
PROSITE; PS50110; RESPONSE_REGULATORY; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell inner membrane; Cell membrane;
Complete proteome; Kinase; Membrane; Nucleotide-binding;
Phosphoprotein; Reference proteome; Signal; Transferase;
Transmembrane; Transmembrane helix; Two-component regulatory system;
Virulence.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 1238 Virulence sensor protein BvgS.
/FTId=PRO_0000032370.
TOPO_DOM 33 307 Cytoplasmic. {ECO:0000255}.
TRANSMEM 308 331 Helical. {ECO:0000255}.
TOPO_DOM 332 541 Periplasmic. {ECO:0000255}.
TRANSMEM 542 563 Helical. {ECO:0000255}.
TOPO_DOM 564 1238 Cytoplasmic. {ECO:0000255}.
DOMAIN 580 651 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 652 708 PAC. {ECO:0000255|PROSITE-
ProRule:PRU00141}.
DOMAIN 726 948 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107}.
DOMAIN 974 1095 Response regulatory.
{ECO:0000255|PROSITE-ProRule:PRU00169}.
DOMAIN 1133 1228 HPt. {ECO:0000255|PROSITE-
ProRule:PRU00110}.
MOD_RES 729 729 Phosphohistidine; by autocatalysis.
{ECO:0000305}.
MOD_RES 1023 1023 4-aspartylphosphate. {ECO:0000305}.
MOD_RES 1172 1172 Phosphohistidine. {ECO:0000305}.
MUTAGEN 729 729 H->Q: Loss of autophosphorylation.
{ECO:0000269|PubMed:8302847}.
MUTAGEN 979 979 D->G: Loss of activity; when associated
with G-980. {ECO:0000269|PubMed:7752227}.
MUTAGEN 980 980 D->G: Loss of activity.
{ECO:0000269|PubMed:7752227}.
MUTAGEN 1023 1023 D->G,N: Loss of activity.
{ECO:0000269|PubMed:7752227,
ECO:0000269|PubMed:8302847}.
MUTAGEN 1080 1080 K->L: Loss of activity.
{ECO:0000269|PubMed:7752227}.
MUTAGEN 1146 1147 Missing: Loss of activity.
MUTAGEN 1172 1172 H->Q: Loss of activity.
{ECO:0000269|PubMed:8605872}.
CONFLICT 705 705 K -> E (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 1068 1068 R -> A (in Ref. 1 and 2). {ECO:0000305}.
STRAND 34 38 {ECO:0000244|PDB:4Q0C}.
HELIX 54 62 {ECO:0000244|PDB:4Q0C}.
STRAND 64 70 {ECO:0000244|PDB:4Q0C}.
TURN 75 77 {ECO:0000244|PDB:4Q0C}.
STRAND 79 81 {ECO:0000244|PDB:4Q0C}.
STRAND 84 87 {ECO:0000244|PDB:4Q0C}.
HELIX 88 99 {ECO:0000244|PDB:4Q0C}.
STRAND 103 111 {ECO:0000244|PDB:4Q0C}.
HELIX 112 120 {ECO:0000244|PDB:4Q0C}.
STRAND 125 130 {ECO:0000244|PDB:4Q0C}.
STRAND 134 137 {ECO:0000244|PDB:4Q0C}.
STRAND 139 142 {ECO:0000244|PDB:4Q0C}.
STRAND 151 156 {ECO:0000244|PDB:4Q0C}.
HELIX 164 167 {ECO:0000244|PDB:4Q0C}.
STRAND 170 175 {ECO:0000244|PDB:4Q0C}.
TURN 176 178 {ECO:0000244|PDB:4Q0C}.
HELIX 181 187 {ECO:0000244|PDB:4Q0C}.
STRAND 191 198 {ECO:0000244|PDB:4Q0C}.
HELIX 199 207 {ECO:0000244|PDB:4Q0C}.
STRAND 212 217 {ECO:0000244|PDB:4Q0C}.
HELIX 218 228 {ECO:0000244|PDB:4Q0C}.
TURN 229 232 {ECO:0000244|PDB:4Q0C}.
STRAND 233 238 {ECO:0000244|PDB:4Q0C}.
STRAND 246 251 {ECO:0000244|PDB:4Q0C}.
HELIX 255 267 {ECO:0000244|PDB:4Q0C}.
HELIX 270 279 {ECO:0000244|PDB:4Q0C}.
HELIX 283 285 {ECO:0000244|PDB:4Q0C}.
TURN 286 288 {ECO:0000244|PDB:4Q0C}.
HELIX 297 305 {ECO:0000244|PDB:3MPK}.
STRAND 307 314 {ECO:0000244|PDB:3MPK}.
TURN 318 320 {ECO:0000244|PDB:3MPK}.
STRAND 321 323 {ECO:0000244|PDB:3MPL}.
STRAND 329 331 {ECO:0000244|PDB:3MPL}.
HELIX 332 344 {ECO:0000244|PDB:3MPK}.
STRAND 347 355 {ECO:0000244|PDB:3MPK}.
HELIX 356 365 {ECO:0000244|PDB:3MPK}.
STRAND 369 375 {ECO:0000244|PDB:3MPK}.
HELIX 378 380 {ECO:0000244|PDB:3MPK}.
TURN 381 383 {ECO:0000244|PDB:3MPK}.
STRAND 384 386 {ECO:0000244|PDB:3MPK}.
STRAND 390 393 {ECO:0000244|PDB:3MPK}.
STRAND 395 402 {ECO:0000244|PDB:3MPK}.
HELIX 409 411 {ECO:0000244|PDB:3MPK}.
STRAND 416 420 {ECO:0000244|PDB:3MPK}.
HELIX 425 432 {ECO:0000244|PDB:3MPK}.
STRAND 436 443 {ECO:0000244|PDB:3MPK}.
HELIX 444 452 {ECO:0000244|PDB:3MPK}.
STRAND 457 462 {ECO:0000244|PDB:3MPK}.
HELIX 463 473 {ECO:0000244|PDB:3MPK}.
TURN 475 477 {ECO:0000244|PDB:3MPK}.
STRAND 478 483 {ECO:0000244|PDB:3MPK}.
STRAND 489 496 {ECO:0000244|PDB:3MPK}.
HELIX 500 511 {ECO:0000244|PDB:3MPK}.
HELIX 515 523 {ECO:0000244|PDB:3MPK}.
HELIX 532 544 {ECO:0000244|PDB:4Q0C}.
SEQUENCE 1238 AA; 135001 MW; 28433439765ABC66 CRC64;
MPAPHRLYPR SLICLAQALL AWALLAWAPA QASQELTLVG KAAVPDVEVA LDGDDWRWLA
RKRVLTLGVY APDIPPFDVT YGERYEGLTA DYMAIIAHNL GMQAKVLRYP TREQALSALE
SGQIDLIGTV NGTDGRQQSL RLSVPYAADH PVIVMPIGAR HVPASNLAGQ RLAVDINYLP
KETLARAYPQ ATLHYFPSSE QALAAVAYGQ ADVFIGDALT TSHLVSQSYF NDVRVVAPAH
IATGGESFGV RADNTRLLRV VNAVLEAIPP SEHRSLIYRW GLGSSISLDF AHPAYSAREQ
QWMADHPVVK VAVLNLFAPF TLFRTDEQFG GISAAVLQLL QLRTGLDFEI IGVDTVEELI
AKLRSGEADM AGALFVNSAR ESFLSFSRPY VRNGMVIVTR QDPDAPVDAD HLDGRTVALV
RNSAAIPLLQ RRYPQAKVVT ADNPSEAMLM VANGQADAVV QTQISASYYV NRYFAGKLRI
ASALDLPPAE IALATTRGQT ELMSILNKAL YSISNDELAS IISRWRGSDG DPRTWYAYRN
EIYLLIGLGL LSALLFLSWI VYLRRQIRQR KRAERALNDQ LEFMRVLIDG TPNPIYVRDK
EGRMLLCNDA YLDTFGVTAD AVLGKTIPEA NVVGDPALAR EMHEFLLTRV AAEREPRFED
RDVTLHGRTR HVYQWTIPYG DSLGELKGII GGWIDITERA ELLRKLHDAK ESADAANRAK
TTFLATMSHE IRTPMNAIIG MLELALLRPT DQEPDRQSIQ VAYDSARSLL ELIGDILDIA
KIEAGKFDLA PVRTALRVLP EGAIRVFDGL ARQKGIELVL KTDIVGVDDV LIDPLRMKQV
LSNLVGNAIK FTTEGQVVLA VTARPDGDAA HVQFSVSDTG CGISEADQRQ LFKPFSQVGG
SAEAGPAPGT GLGLSISRRL VELMGGTLVM RSAPGVGTTV SVDLRLTMVE KSVQAAPPAA
ATAATPSKPQ VSLRVLVVDD HKPNLMLLRQ QLDYLGQRVI AADSGEAALA LWREHAFDVV
ITDCNMPGIS GYELARRIRA AEAAPGYGRT RCILFGFTAS AQMDEAQRCR AAGMDDCLFK
PIGVDALRQR LNEAVARAAL PTPPSPQAAA PATDDATPTA FSAESILALT QNDEALIRQL
LEEVIRTNRA DVDQLQKLHQ QADWPKVSDM AHRLAGGARV VDAKAMIDTV LALEKKAQGQ
AGPSPEIDGL VRTLAAQSAA LETQLRAWLE QRPHQDQP


Related products :

Catalog number Product name Quantity
EIAAB39251 C9orf80,Homo sapiens,HSPC043,HSPC291,hSSBIP1,Human,Sensor of single-strand DNA complex subunit C,Sensor of ssDNA subunit C,Single-stranded DNA-binding protein-interacting protein 1,SOSS complex subuni
EIAAB39241 Homo sapiens,hSSB1,Human,LP3587,OBFC2B,Oligonucleotide_oligosaccharide-binding fold-containing protein 2B,Sensor of single-strand DNA complex subunit B1,Sensor of ssDNA subunit B1,Single-stranded DNA-
EIAAB39242 Bos taurus,Bovine,OBFC2A,Oligonucleotide_oligosaccharide-binding fold-containing protein 2A,Sensor of single-strand DNA complex subunit B2,Sensor of ssDNA subunit B2,Single-stranded DNA-binding protei
EIAAB39239 Mouse,Mus musculus,Nabp2,Obfc2b,Oligonucleotide_oligosaccharide-binding fold-containing protein 2B,Sensor of single-strand DNA complex subunit B1,Sensor of ssDNA subunit B1,Single-stranded DNA-binding
EIAAB39245 Mouse,Mus musculus,Nabp1,Obfc2a,Oligonucleotide_oligosaccharide-binding fold-containing protein 2A,Sensor of single-strand DNA complex subunit B2,Sensor of ssDNA subunit B2,Single-stranded DNA-binding
EIAAB39240 Bos taurus,Bovine,OBFC2B,Oligonucleotide_oligosaccharide-binding fold-containing protein 2B,Sensor of single-strand DNA complex subunit B1,Sensor of ssDNA subunit B1,Single-stranded DNA-binding protei
EIAAB39244 Obfc2a,Oligonucleotide_oligosaccharide-binding fold-containing protein 2A,Rat,Rattus norvegicus,Sensor of single-strand DNA complex subunit B2,Sensor of ssDNA subunit B2,Single-stranded DNA-binding pr
EIAAB39238 Obfc2b,Oligonucleotide_oligosaccharide-binding fold-containing protein 2B,Rat,Rattus norvegicus,Sensor of single-strand DNA complex subunit B1,Sensor of ssDNA subunit B1,Single-stranded DNA-binding pr
EIAAB39243 Homo sapiens,hSSB2,Human,OBFC2A,Oligonucleotide_oligosaccharide-binding fold-containing protein 2A,Sensor of single-strand DNA complex subunit B2,Sensor of ssDNA subunit B2,Single-stranded DNA-binding
EIAAB39252 Mouse,Mus musculus,Sensor of single-strand DNA complex subunit C,Sensor of ssDNA subunit C,Single-stranded DNA-binding protein-interacting protein 1,SOSS complex subunit C,SOSS-C,SSB-interacting prote
EIAAB39250 Bos taurus,Bovine,Sensor of single-strand DNA complex subunit C,Sensor of ssDNA subunit C,Single-stranded DNA-binding protein-interacting protein 1,SOSS complex subunit C,SOSS-C,SSB-interacting protei
EIAAB39253 Chicken,Gallus gallus,RCJMB04_21d4,Sensor of single-strand DNA complex subunit C,Sensor of ssDNA subunit C,Single-stranded DNA-binding protein-interacting protein 1,SOSS complex subunit C,SOSS-C,SSB-i
TS 134 K L VIRULENCE ENRICHMENT (20ml _vl) (Store below 8º C) 5 vl
BF096 *Diphtheria Virulence Supplement (Part A & B) Qty per Litre of Medium:
BF096 Diphtheria Virulence Supplement (Part A & B) 5x500gm
BF049 KL Virulence Enrichment (20ml per vial) 5x500gm
BF049 *KL Virulence Enrichment (20ml per vial) Qty per Litre of Medium:
0100-0190 SHEEP ANTI NEURONAL CALCIUM SENSOR 1 (C_TERMINAL), Product Type Polyclonal Antibody, Specificity NEURONAL CALCIUM SENSOR 1 , Target Species Rat, Host Sheep, Format Purified, Isotypes Polyclonal 1 ml
SCH-0100-0190 SHEEP ANTI NEURONAL CALCIUM SENSOR 1 (C_TERMINAL), Product Type Polyclonal Antibody, Specificity NEURONAL CALCIUM SENSOR 1 , Target Species Rat, Host Sheep, Format Purified, Isotypes Polyclonal 1 ml
3915 H5N1, virulence factor, dsRNA, RNase L 0.5 mg
3915 H5N1, virulence factor, dsRNA, RNase L 0.1 mg
TS 059 DIPHTHERIA VIRULENCE SUPPLEMENT (Part A & B) DOUBLE PACK (Store below 8º C) 1 vl
U0291h CLIA C1orf193,C1orf60,Homo sapiens,Human,Int3,Integrator complex subunit 3,INTS3,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 96T
E0291h ELISA kit C1orf193,C1orf60,Homo sapiens,Human,Int3,Integrator complex subunit 3,INTS3,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 96T
E0291h ELISA C1orf193,C1orf60,Homo sapiens,Human,Int3,Integrator complex subunit 3,INTS3,Sensor of single-strand DNA complex subunit A,Sensor of ssDNA subunit A,SOSS complex subunit A,SOSS-A 96T


 

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