⊟Summary[edit | edit source]
- pan ID?: SAUPAN000975000
- symbol?: capB
- synonym:
- description?: capsular polysaccharide biosynthesis protein Cap5B
- capsular polysaccharide biosynthesis protein Cap5B
- capsular polysaccharide biosynthesis protein CapB
- capsular polysaccharide synthesis enzyme CapB
- capsular polysaccharide synthesis protein Cap5B
- type 8 capsular polysaccharide synthesis protein Cap8B
- tyrosine-protein kinase
- capsular polysaccharide synthesis enzyme Cap5B
- capsular polysaccharide synthesis enzyme Cap8B
- exopolysaccharide tyrosine-protein kinase
- Non-specific protein-tyrosine kinase
- putative tyrosine-protein kinase capB
- Tyrosine-protein kinase (capsular polysaccharide biosynthesis)
- Tyrosine-protein kinase EpsD / Capsular polysaccharide synthesis enzyme Cap5B
- tyrosine-protein kinase YwqD
descriptions from strain specific annotations:
- strand?: +
- coordinates?: 1231298..1231993
- synteny block?: BlockID0005090
- occurrence?: in 100% of 34 strains
capB1 : capsular polysaccharide copolymerase/tyrosine kinase CapB1 [1]
• A crystal structure is available : 4JLV
The capsule regulatory system is not intuitive and has conflicting literature. CapAB forms a bacterial tyrosine kinase (BTY) system that uses a transmembrane stimulatory protein (CapA1) to induce oligomerization of its cognate tyrosine kinase (CapB1) which as an oligomer undergoes autophosphorylation, dissociates from the complex, phosphorylates target enzymes (CapE, CapM, CapO), and activates their catalytic activity. The CapAB membrane oligomerization state appears to regulate CapK flippase activity and/or CapJ polymerase activity. The CapB1 autophosphorylation rate can be regulated by the serine-threonine kinase PknB. Contrary to previous reports, CapB1 is a functional tyrosine kinase and is essential for capsule biosynthesis; its paralogue CapB2 is not required for capsule production.
Historically, different capsule types were assigned their own nomenclature (i.e. Cap5B1 and Cap8B1 for the two most prevalent capsule types, CP5 and CP8). The CapB1 protein is 97% identical between Cap5B1 and Cap8B1, provides the same function, and is therefore harmonized as CapB1.
⊟Orthologs[edit | edit source]
⊟Genome Viewer[edit | edit source]
| COL | |
| N315 | |
| NCTC8325 | |
| Newman | |
| USA300_FPR3757 |
⊟Alignments[edit | edit source]
- alignment of orthologues: CLUSTAL format alignment by MAFFT L-INS-i (v7.307)
COL ---MSKKENTTTTLFVYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKST
N315 ---MSKKENTTTTLFVYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKST
NCTC8325 ---MSKKENTTTTLFVYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKST
Newman MLLMSKKENTTTTLFVYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKST
USA300_FPR3757 ---MSKKENTTTTLFVYEKPKSTISEKFRGIRSNIMFSKANGEVKRLLVTSEKPGAGKST
*********************************************************
COL VVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIE
N315 VVSNVAITYAQAGYKTLVIDGDMCKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIE
NCTC8325 VVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIE
Newman VVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIE
USA300_FPR3757 VVSNVAITYAQAGYKTLVIDGDMRKPTQNYIFNEQNNNGLSSLIIGRTTMSEAITSTEIE
*********************** ************************************
COL NLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDS
N315 NLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDS
NCTC8325 NLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDS
Newman NLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDS
USA300_FPR3757 NLDLLTAGPVPPNPSELIGSERFKELVDLFNKRYDIIIVDTPPVNTVTDAQLYARAIKDS
************************************************************
COL LLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKTKVDKSSSYYHYYGDE
N315 LLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKTKVDKSSSYYHYYGDE
NCTC8325 LLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKTKVDKSSSYYHYYGDE
Newman LLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKTKVDKSSSYYHYYGDE
USA300_FPR3757 LLVIDSEKNDKNEVKKAKALMEKAGSNILGVILNKTKVDKSSSYYHYYGDE
***************************************************
- ↑ Vanesa Olivares-Illana, Philippe Meyer, Emmanuelle Bechet, Virginie Gueguen-Chaignon, Didier Soulat, Sylvie Lazereg-Riquier, Ivan Mijakovic, Josef Deutscher, Alain J Cozzone, Olivier Laprévote, Solange Morera, Christophe Grangeasse, Sylvie Nessler
Structural basis for the regulation mechanism of the tyrosine kinase CapB from Staphylococcus aureus.
PLoS Biol: 2008, 6(6);e143
[PubMed:18547145] [WorldCat.org] [DOI] (I p)Jakub Gruszczyk, Vanesa Olivares-Illana, Julien Nourikyan, Aurore Fleurie, Emmanuelle Béchet, Virginie Gueguen-Chaignon, Céline Freton, Magali Aumont-Nicaise, Solange Moréra, Christophe Grangeasse, Sylvie Nessler
Comparative analysis of the Tyr-kinases CapB1 and CapB2 fused to their cognate modulators CapA1 and CapA2 from Staphylococcus aureus.
PLoS One: 2013, 8(10);e75958
[PubMed:24146800] [WorldCat.org] [DOI] (I e)Marvin Rausch, Julia P Deisinger, Hannah Ulm, Anna Müller, Wenjin Li, Patrick Hardt, Xiaogang Wang, Xue Li, Marc Sylvester, Marianne Engeser, Waldemar Vollmer, Christa E Müller, Hans Georg Sahl, Jean Claire Lee, Tanja Schneider
Coordination of capsule assembly and cell wall biosynthesis in Staphylococcus aureus.
Nat Commun: 2019, 10(1);1404
[PubMed:30926919] [WorldCat.org] [DOI] (I e)Satsawat Visansirikul, Stephen A Kolodziej, Alexei V Demchenko
Staphylococcus aureus capsular polysaccharides: a structural and synthetic perspective.
Org Biomol Chem: 2020, 18(5);783-798
[PubMed:31922180] [WorldCat.org] [DOI] (I p)