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Penicillin-binding protein 1B (PBP-1b) (PBP1b) (Murein polymerase) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase) (Peptidoglycan glycosyltransferase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase)]

 PBPB_ECOLI              Reviewed;         844 AA.
P02919; P75664;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
19-JUL-2003, sequence version 2.
28-MAR-2018, entry version 194.
RecName: Full=Penicillin-binding protein 1B;
Short=PBP-1b;
Short=PBP1b;
AltName: Full=Murein polymerase;
Includes:
RecName: Full=Penicillin-insensitive transglycosylase;
EC=2.4.1.129 {ECO:0000269|PubMed:19458048, ECO:0000269|PubMed:6389538};
AltName: Full=Peptidoglycan TGase;
AltName: Full=Peptidoglycan glycosyltransferase;
Includes:
RecName: Full=Penicillin-sensitive transpeptidase;
EC=3.4.16.4 {ECO:0000269|PubMed:6389538};
AltName: Full=DD-transpeptidase;
Name=mrcB; Synonyms=pbpF, ponB; OrderedLocusNames=b0149, JW0145;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=3882429; DOI=10.1111/j.1432-1033.1985.tb08768.x;
Broome-Smith J.K., Edelman A., Yousif S., Spratt B.G.;
"The nucleotide sequences of the ponA and ponB genes encoding
penicillin-binding protein 1A and 1B of Escherichia coli K12.";
Eur. J. Biochem. 147:437-446(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8202364; DOI=10.1093/nar/22.9.1637;
Fujita N., Mori H., Yura T., Ishihama A.;
"Systematic sequencing of the Escherichia coli genome: analysis of the
2.4-4.1 min (110,917-193,643 bp) region.";
Nucleic Acids Res. 22:1637-1639(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
TO 103 AND 754.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 497-525.
STRAIN=K12;
PubMed=3920658; DOI=10.1073/pnas.82.7.1999;
Keck W., Glauner B., Schwarz U., Broome-Smith J.K., Spratt B.G.;
"Sequences of the active-site peptides of three of the high-Mr
penicillin-binding proteins of Escherichia coli K-12.";
Proc. Natl. Acad. Sci. U.S.A. 82:1999-2003(1985).
[6]
CATALYTIC ACTIVITY.
PubMed=6389538;
Nakagawa J., Tamaki S., Tomioka S., Matsuhashi M.;
"Functional biosynthesis of cell wall peptidoglycan by polymorphic
bifunctional polypeptides. Penicillin-binding protein 1Bs of
Escherichia coli with activities of transglycosylase and
transpeptidase.";
J. Biol. Chem. 259:13937-13946(1984).
[7]
CHARACTERIZATION.
PubMed=8645198; DOI=10.1042/bj3160149;
Wang C.C., Schultz D.R., Nicholas R.A.;
"Localization of a putative second membrane association site in
penicillin-binding protein 1B of Escherichia coli.";
Biochem. J. 316:149-156(1996).
[8]
TOPOLOGY.
PubMed=9244263; DOI=10.1128/jb.179.15.4761-4767.1997;
Lefevre F., Remy M.-H., Masson J.-M.;
"Topographical and functional investigation of Escherichia coli
penicillin-binding protein 1b by alanine stretch scanning
mutagenesis.";
J. Bacteriol. 179:4761-4767(1997).
[9]
TOPOLOGY.
PubMed=3330753; DOI=10.1111/j.1365-2958.1987.tb00533.x;
Edelman A., Bowler L., Broome-Smith J.K., Spratt B.G.;
"Use of a beta-lactamase fusion vector to investigate the organization
of penicillin-binding protein 1B in the cytoplasmic membrane of
Escherichia coli.";
Mol. Microbiol. 1:101-106(1987).
[10]
DIMERIZATION.
PubMed=1885547; DOI=10.1128/jb.173.18.5740-5746.1991;
Zijderveld C.A., Aarsman M.E., den Blaauwen T., Nanninga N.;
"Penicillin-binding protein 1B of Escherichia coli exists in dimeric
forms.";
J. Bacteriol. 173:5740-5746(1991).
[11]
INTERACTION WITH MIPA AND MLTA.
STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
PubMed=10037771; DOI=10.1074/jbc.274.10.6726;
Vollmer W., von Rechenberg M., Hoeltje J.-V.;
"Demonstration of molecular interactions between the murein polymerase
PBP1B, the lytic transglycosylase MltA, and the scaffolding protein
MipA of Escherichia coli.";
J. Biol. Chem. 274:6726-6734(1999).
[12]
ACTIVE SITE SER-510, AND MUTAGENESIS OF GLU-233; ASP-234 AND GLU-290.
STRAIN=EJ801;
PubMed=10564478; DOI=10.1046/j.1365-2958.1999.01612.x;
Terrak M., Ghosh T.K., van Heijenoort J., Van Beeumen J., Lampilas M.,
Aszodi J., Ayala J.A., Ghuysen J.-M., Nguyen-Disteche M.;
"The catalytic, glycosyl transferase and acyl transferase modules of
the cell wall peptidoglycan-polymerizing penicillin-binding protein 1b
of Escherichia coli.";
Mol. Microbiol. 34:350-364(1999).
[13]
REVIEW.
PubMed=9841666;
Goffin C., Ghuysen J.-M.;
"Multimodular penicillin-binding proteins: an enigmatic family of
orthologs and paralogs.";
Microbiol. Mol. Biol. Rev. 62:1079-1093(1998).
[14]
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 58-804 IN COMPLEX WITH
MOENOMYCIN, PARTIAL PROTEIN SEQUENCE, INTERACTION WITH MLTA; UVRA;
FTSL AND FTSN, MEMBRANE TOPOLOGY, CATALYTIC ACTIVITY, DOMAIN, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=19458048; DOI=10.1073/pnas.0904030106;
Sung M.-T., Lai Y.-T., Huang C.-Y., Chou L.-Y., Shih H.-W.,
Cheng W.-C., Wong C.-H., Ma C.;
"Crystal structure of the membrane-bound bifunctional transglycosylase
PBP1b from Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 106:8824-8829(2009).
-!- FUNCTION: Cell wall formation. Synthesis of cross-linked
peptidoglycan from the lipid intermediates. The enzyme has a
penicillin-insensitive transglycosylase N-terminal domain
(formation of linear glycan strands) and a penicillin-sensitive
transpeptidase C-terminal domain (cross-linking of the peptide
subunits).
-!- CATALYTIC ACTIVITY: (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-
Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-
diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-
Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl
diphosphate. {ECO:0000269|PubMed:19458048,
ECO:0000269|PubMed:6389538}.
-!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
N-acyl substituents of D-alanine. {ECO:0000269|PubMed:6389538}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBUNIT: Forms a trimeric complex with MipA and MltA. Has also
been shown to exist as monomer or homodimer; homodimer of Alpha
and Gamma isozymes can be found. Interacts with UvrA, FtsL and
FtsN. {ECO:0000269|PubMed:10037771, ECO:0000269|PubMed:19458048}.
-!- INTERACTION:
P0AD68:ftsI; NbExp=3; IntAct=EBI-909769, EBI-548564;
P29131:ftsN; NbExp=7; IntAct=EBI-909769, EBI-1134233;
P0AB38:lpoB; NbExp=4; IntAct=EBI-909769, EBI-3405489;
-!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass type II
membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Alpha; Synonyms=Long;
IsoId=P02919-1; Sequence=Displayed;
Name=Gamma; Synonyms=Short;
IsoId=P02919-2; Sequence=VSP_018737;
-!- DOMAIN: The UvrB domain 2 homolog region (UB2H domain) is
important for interaction with MltA.
{ECO:0000269|PubMed:19458048}.
-!- MISCELLANEOUS: A third isozyme, Beta, lacking the first 25 N-
terminal amino acids of the isoform Alpha and a fourth isozyme,
Delta, have been found, but seem to result from the artifactual
degradation of the isoform Alpha and isoform Gamma respectively.
-!- SIMILARITY: In the N-terminal section; belongs to the
glycosyltransferase 51 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the
transpeptidase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA26099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X02163; CAA26098.1; -; Genomic_DNA.
EMBL; X02163; CAA26099.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC73260.1; -; Genomic_DNA.
EMBL; AP009048; BAB96725.2; -; Genomic_DNA.
PIR; E64738; ZPECPB.
RefSeq; NP_414691.1; NC_000913.3.
RefSeq; WP_000918162.1; NZ_LN832404.1.
PDB; 3FWL; X-ray; 3.09 A; A=58-804.
PDB; 3VMA; X-ray; 2.16 A; A=58-804.
PDB; 5FGZ; X-ray; 2.85 A; A=58-804.
PDB; 5HL9; X-ray; 2.70 A; A=58-804.
PDB; 5HLA; X-ray; 2.36 A; A=58-804.
PDB; 5HLB; X-ray; 2.42 A; A=58-804.
PDB; 5HLD; X-ray; 2.31 A; A=58-804.
PDBsum; 3FWL; -.
PDBsum; 3VMA; -.
PDBsum; 5FGZ; -.
PDBsum; 5HL9; -.
PDBsum; 5HLA; -.
PDBsum; 5HLB; -.
PDBsum; 5HLD; -.
ProteinModelPortal; P02919; -.
SMR; P02919; -.
BioGrid; 4260880; 259.
DIP; DIP-10252N; -.
IntAct; P02919; 15.
STRING; 316385.ECDH10B_0129; -.
BindingDB; P02919; -.
ChEMBL; CHEMBL1814; -.
DrugBank; DB01414; Cefacetrile.
DrugBank; DB01327; Cefazolin.
DrugBank; DB00274; Cefmetazole.
DrugBank; DB01328; Cefonicid.
DrugBank; DB01329; Cefoperazone.
DrugBank; DB01331; Cefoxitin.
DrugBank; DB00430; Cefpiramide.
DrugBank; DB00438; Ceftazidime.
DrugBank; DB01415; Ceftibuten.
DrugBank; DB01332; Ceftizoxime.
DrugBank; DB06211; Doripenem.
DrugBank; DB00303; Ertapenem.
DrugBank; DB01598; Imipenem.
DrugBank; DB04570; Latamoxef.
CAZy; GT51; Glycosyltransferase Family 51.
PaxDb; P02919; -.
PRIDE; P02919; -.
EnsemblBacteria; AAC73260; AAC73260; b0149.
EnsemblBacteria; BAB96725; BAB96725; BAB96725.
GeneID; 944843; -.
KEGG; ecj:JW0145; -.
KEGG; eco:b0149; -.
PATRIC; fig|1411691.4.peg.2132; -.
EchoBASE; EB0600; -.
EcoGene; EG10605; mrcB.
eggNOG; ENOG4105BZ4; Bacteria.
eggNOG; COG0744; LUCA.
HOGENOM; HOG000282711; -.
InParanoid; P02919; -.
KO; K05365; -.
OMA; VHGMGLA; -.
PhylomeDB; P02919; -.
BioCyc; EcoCyc:EG10605-MONOMER; -.
BioCyc; MetaCyc:EG10605-MONOMER; -.
BRENDA; 2.4.1.129; 2026.
UniPathway; UPA00219; -.
EvolutionaryTrace; P02919; -.
PRO; PR:P02919; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
GO; GO:0009274; C:peptidoglycan-based cell wall; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0008144; F:drug binding; IDA:EcoCyc.
GO; GO:0071723; F:lipopeptide binding; IPI:EcoCyc.
GO; GO:0008658; F:penicillin binding; IDA:EcoCyc.
GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IDA:EcoCyc.
GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IDA:EcoCyc.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IDA:EcoCyc.
GO; GO:0008360; P:regulation of cell shape; IGI:EcoCyc.
GO; GO:0046677; P:response to antibiotic; IGI:EcoCyc.
GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
Gene3D; 1.10.3810.10; -; 2.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR001264; Glyco_trans_51.
InterPro; IPR023346; Lysozyme-like_dom_sf.
InterPro; IPR032730; PBP1b_TM.
InterPro; IPR011813; PBP_1b.
InterPro; IPR036950; PBP_transglycosylase.
InterPro; IPR001460; PCN-bd_Tpept.
InterPro; IPR028166; UB2H.
Pfam; PF14812; PBP1_TM; 1.
Pfam; PF00912; Transgly; 1.
Pfam; PF00905; Transpeptidase; 1.
Pfam; PF14814; UB2H; 1.
PIRSF; PIRSF002799; PBP_1b; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF56601; SSF56601; 2.
TIGRFAMs; TIGR02071; PBP_1b; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Antibiotic resistance;
Carboxypeptidase; Cell inner membrane; Cell membrane; Cell shape;
Cell wall biogenesis/degradation; Complete proteome;
Direct protein sequencing; Glycosyltransferase; Hydrolase; Membrane;
Multifunctional enzyme; Peptidoglycan synthesis; Protease;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix.
CHAIN 1 844 Penicillin-binding protein 1B.
/FTId=PRO_0000012145.
TOPO_DOM 1 63 Cytoplasmic. {ECO:0000305}.
TRANSMEM 64 87 Helical; Signal-anchor for type II
membrane protein. {ECO:0000305}.
TOPO_DOM 88 844 Periplasmic. {ECO:0000305}.
REGION 88 250 Membrane association.
REGION 109 200 UvrB domain 2 homolog.
REGION 195 367 Transglycosylase.
REGION 444 736 Transpeptidase.
ACT_SITE 233 233 Proton donor; for transglycosylase
activity. {ECO:0000305|PubMed:10564478}.
ACT_SITE 510 510 Acyl-ester intermediate; for
transpeptidase activity.
{ECO:0000269|PubMed:10564478}.
VAR_SEQ 1 45 Missing (in isoform Gamma).
{ECO:0000305}.
/FTId=VSP_018737.
MUTAGEN 233 233 E->Q: Loss of wild-type glycan chain
elongation activity. No complementation
in strain defective in PBP-1b.
{ECO:0000269|PubMed:10564478}.
MUTAGEN 234 234 D->N: 7-fold decrease in catalytic
activity. No complementation in strain
defective in PBP-1b.
{ECO:0000269|PubMed:10564478}.
MUTAGEN 290 290 E->Q: 11-fold decrease in catalytic
activity. Shows complementation activity
in strain defective in PBP-1b.
{ECO:0000269|PubMed:10564478}.
CONFLICT 103 103 P -> A (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 754 754 P -> PTP (in Ref. 2). {ECO:0000305}.
TURN 69 72 {ECO:0000244|PDB:3FWL}.
HELIX 76 88 {ECO:0000244|PDB:3VMA}.
HELIX 90 93 {ECO:0000244|PDB:3VMA}.
STRAND 104 107 {ECO:0000244|PDB:3VMA}.
STRAND 111 113 {ECO:0000244|PDB:5HL9}.
HELIX 121 130 {ECO:0000244|PDB:3VMA}.
STRAND 144 148 {ECO:0000244|PDB:3VMA}.
STRAND 151 156 {ECO:0000244|PDB:3VMA}.
STRAND 159 161 {ECO:0000244|PDB:3VMA}.
STRAND 164 166 {ECO:0000244|PDB:3VMA}.
STRAND 169 176 {ECO:0000244|PDB:3VMA}.
STRAND 179 185 {ECO:0000244|PDB:3VMA}.
TURN 186 189 {ECO:0000244|PDB:3VMA}.
STRAND 193 196 {ECO:0000244|PDB:3VMA}.
STRAND 201 205 {ECO:0000244|PDB:3VMA}.
STRAND 210 212 {ECO:0000244|PDB:3VMA}.
HELIX 218 220 {ECO:0000244|PDB:5HLD}.
HELIX 223 231 {ECO:0000244|PDB:3VMA}.
STRAND 234 236 {ECO:0000244|PDB:3VMA}.
STRAND 237 239 {ECO:0000244|PDB:3FWL}.
HELIX 241 243 {ECO:0000244|PDB:3FWL}.
TURN 247 249 {ECO:0000244|PDB:3VMA}.
HELIX 268 276 {ECO:0000244|PDB:3VMA}.
STRAND 280 282 {ECO:0000244|PDB:5FGZ}.
HELIX 284 300 {ECO:0000244|PDB:3VMA}.
HELIX 303 310 {ECO:0000244|PDB:3VMA}.
TURN 311 313 {ECO:0000244|PDB:3VMA}.
STRAND 314 319 {ECO:0000244|PDB:3VMA}.
STRAND 322 326 {ECO:0000244|PDB:3VMA}.
HELIX 327 335 {ECO:0000244|PDB:3VMA}.
HELIX 339 341 {ECO:0000244|PDB:3VMA}.
HELIX 344 355 {ECO:0000244|PDB:3VMA}.
STRAND 356 360 {ECO:0000244|PDB:3VMA}.
TURN 362 364 {ECO:0000244|PDB:3VMA}.
HELIX 366 382 {ECO:0000244|PDB:3VMA}.
STRAND 383 385 {ECO:0000244|PDB:5HLB}.
HELIX 388 395 {ECO:0000244|PDB:3VMA}.
STRAND 408 411 {ECO:0000244|PDB:3VMA}.
HELIX 412 426 {ECO:0000244|PDB:3VMA}.
TURN 430 432 {ECO:0000244|PDB:5HLD}.
STRAND 433 435 {ECO:0000244|PDB:3VMA}.
STRAND 437 440 {ECO:0000244|PDB:3VMA}.
HELIX 444 464 {ECO:0000244|PDB:3VMA}.
STRAND 471 478 {ECO:0000244|PDB:3VMA}.
TURN 479 481 {ECO:0000244|PDB:3VMA}.
STRAND 483 488 {ECO:0000244|PDB:3VMA}.
STRAND 490 492 {ECO:0000244|PDB:5HL9}.
STRAND 493 495 {ECO:0000244|PDB:5HLD}.
HELIX 500 503 {ECO:0000244|PDB:3VMA}.
HELIX 509 512 {ECO:0000244|PDB:3VMA}.
HELIX 513 521 {ECO:0000244|PDB:3VMA}.
TURN 524 526 {ECO:0000244|PDB:3VMA}.
STRAND 532 534 {ECO:0000244|PDB:3VMA}.
STRAND 540 542 {ECO:0000244|PDB:5HL9}.
STRAND 543 545 {ECO:0000244|PDB:3VMA}.
STRAND 546 548 {ECO:0000244|PDB:5HL9}.
STRAND 561 564 {ECO:0000244|PDB:3VMA}.
HELIX 565 570 {ECO:0000244|PDB:3VMA}.
HELIX 574 584 {ECO:0000244|PDB:3VMA}.
HELIX 586 596 {ECO:0000244|PDB:3VMA}.
HELIX 600 602 {ECO:0000244|PDB:3VMA}.
HELIX 607 611 {ECO:0000244|PDB:3VMA}.
HELIX 618 629 {ECO:0000244|PDB:3VMA}.
STRAND 632 634 {ECO:0000244|PDB:3VMA}.
STRAND 640 644 {ECO:0000244|PDB:3VMA}.
STRAND 646 648 {ECO:0000244|PDB:3FWL}.
STRAND 650 653 {ECO:0000244|PDB:3VMA}.
HELIX 664 679 {ECO:0000244|PDB:3VMA}.
HELIX 684 689 {ECO:0000244|PDB:3VMA}.
HELIX 691 693 {ECO:0000244|PDB:3VMA}.
STRAND 696 701 {ECO:0000244|PDB:3VMA}.
HELIX 703 705 {ECO:0000244|PDB:3VMA}.
STRAND 706 713 {ECO:0000244|PDB:3VMA}.
STRAND 715 724 {ECO:0000244|PDB:3VMA}.
HELIX 737 749 {ECO:0000244|PDB:3VMA}.
STRAND 763 768 {ECO:0000244|PDB:3VMA}.
STRAND 774 777 {ECO:0000244|PDB:3VMA}.
STRAND 780 786 {ECO:0000244|PDB:3VMA}.
HELIX 792 797 {ECO:0000244|PDB:3VMA}.
SEQUENCE 844 AA; 94293 MW; CED0A19FAC73961E CRC64;
MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG KGKGKGRKPR
GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW QLPAAVYGRM VNLEPDMTIS
KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL
ATIVNMENNR QFGFFRLDPR LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH
DGISLYSIGR AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL VGMVKGASIY
NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG VQPRGGVISP QPAFMQLVRQ
ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF
SGEVRAMVGG SEPQFAGYNR AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL
RQPNGQVWSP QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV LYQSFPQAER
AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG TTNNNVDTWF AGIDGSTVTI
TWVGRDNNQP TKLYGASGAM SIYQRYLANQ TPTPLNLVPP EDIADMGVDY DGNFVCSGGM
RILPVWTSDP QSLCQQSEMQ QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM
FGSN


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AS11 1657 Antibody: Penicillin G, Total IgG (2.5mg), Immunogen: penicillin G , Host: rabbit , polyclonal, Confirmed reactivity: penicillin G (100 percent ), penicillin acid (90 percent ), cloxacillin (110 2.5 mg
AS11 1731 Antibody: Penicillin G, Serum (1ml), Immunogen: penicillin G , Host: rabbit , polyclonal, Confirmed reactivity: penicillin G (100 percent ), penicillin acid (90 percent ), cloxacillin (110 percen 1 ml
AS11 1642 Antibody: Penicillin G, Serum (0.1ml), Immunogen: penicillin G, Host: rabbit, polyclonal, Confirmed reactivity: penicillin G (100 percent ), penicillin acid (90 percent ), cloxacillin (110 percent ), 0.1 ml
AS11 1646 Antibody: Penicillin V, Total IgG (1 mg), Immunogen: penicillin V , Host: rabbit , polyclonal, Confirmed reactivity: penicillin V (100 percent ), cloxacillin (90 percent ), dicloxacillin (80 percen 1 mg
AS11 1751 Antibody: Penicillin V (0.2 mg total IgG), Immunogen: penicillin V , Host: rabbit , polyclonal, Confirmed reactivity: penicillin V (100 percent ), cloxacillin (90 percent ), dicloxacillin (80 perce 2.5 mg
AS11 1661 Antibody: Penicillin V, Serum (0.1 ml), Immunogen: penicillin V , Host: rabbit , polyclonal, Confirmed reactivity: penicillin V (100 percent ), cloxacillin (90 percent ), dicloxacillin (80 percent 0.1 ml
AS11 1657 Antibody: Penicillin G, Total IgG (2.5mg) , Host: rabbit , polyclonal, Comfirmed reactivity: penicillin G (100 percent ), penicillin acid (90 percent ), cloxacillin (110 percent ), dicloxacillin (70 2.5 mg
AS11 1661 Antibody: Penicillin V, Serum (0.1 ml) , Host: rabbit , polyclonal, Comfirmed reactivity: penicillin V (100 percent ), cloxacillin (90 percent ), dicloxacillin (80 percent ), penicillin G (20 percen 0.1 ml
AS11 1694 Antibody: Penicillin V, Serum (1 ml), Immunogen: penicillin V , Host: rabbit , polyclonal, Confirmed reactivity: penicillin V (100 percent ), cloxacillin (90 percent ), dicloxacillin (80 percent ), 1 ml
AS11 1751 Antibody: Penicillin V (0.2 mg total IgG) , Host: rabbit , polyclonal, Comfirmed reactivity: penicillin V (100 percent ), cloxacillin (90 percent ), dicloxacillin (80 percent ), penicillin G (20 per 2.5 mg
AS11 1642 Antibody: Penicillin G, Serum (0.1ml) , Host: rabbit, polyclonal, Comfirmed reactivity: penicillin G (100 percent ), penicillin acid (90 percent ), cloxacillin (110 percent ), dicloxacillin (70 percen 0.1 ml
AS11 1731 Antibody: Penicillin G, Serum (1ml) , Host: rabbit , polyclonal, Comfirmed reactivity: penicillin G (100 percent ), penicillin acid (90 percent ), cloxacillin (110 percent ), dicloxacillin (70 perce 1 ml
AE81025PE Penicillin G (benzyl penicillin) ELISA Kit 96T
69-57-8 Penicillin Series (Penicillin G Procaine_P - 1g
SCH-7219-9959 MOUSE ANTI PENICILLIN, Product Type Monoclonal Antibody, Specificity PENICILLIN, Target Species Fungal, Host Mouse, Format Purified, Isotypes IgG1, Applications E, Clone Pen_9 0.2 mg
7219-9959 MOUSE ANTI PENICILLIN, Product Type Monoclonal Antibody, Specificity PENICILLIN, Target Species Fungal, Host Mouse, Format Purified, Isotypes IgG1, Applications E, Clone Pen_9 0.2 mg
7220-0004 SHEEP ANTI PENICILLIN, Product Type Polyclonal Antibody, Specificity PENICILLIN, Target Species Fungal, Host Sheep, Format Serum, Isotypes Polyclonal IgG, Applications E, R, Clone 0.2 ml
SCH-7220-0004 SHEEP ANTI PENICILLIN, Product Type Polyclonal Antibody, Specificity PENICILLIN, Target Species Fungal, Host Sheep, Format Serum, Isotypes Polyclonal IgG, Applications E, R, Clone 0.2 ml
Mab-00819 Penicillin, Penicillin
1406-05-9 Penicillin Penicillin 1g
Mab-00818 Penicillin, Penicillin
orb62246 procaine penicillin procaine penicillin For research use only. 500 g
30034-13-0 Penicillin G sulfoxide p-methoxybenzyl e Penicillin G sulfoxide p- 1g
B280 PM Indicator Agar (Penicillin In Milk Indicator Agar) USE For rapid detection of trace amounts of Penicillin in milk as per AOAC. Qty per Litre of Medium: 32


 

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