From DrugPedia: A Wikipedia for Drug discovery

Immunotation of Rv0016c
Name
<Rv0015c>transmembrane serine/threonine-protein kinase A pknA
Identifiers
Swiss Prot	P65726
Genbank	885953
PDB	structure available No structure available
Chemical data
Formula	?
Mol. wt.	45598
Pharmacokinetic data
Bioavailability	?
Solubility	?
Isoelectric-Point	11.1868

=General=The bacterial divisome is a multiprotein complex. Specific protein-protein interactions specify whether cell division occurs optimally, or whether division is arrested. Little is known about these protein-protein interactions and their regulation in mycobacteria. We have investigated the interrelationship between the products of the Mycobacterium tuberculosis gene cluster Rv0014c-Rv0019c, namely PknA (encoded by Rv0014c) and FtsZ-interacting protein A, FipA (encoded by Rv0019c) and the products of the division cell wall (dcw) cluster, namely FtsZ and FtsQ. M. smegmatis strains depleted in components of the two gene clusters have been complemented with orthologs of the respective genes of M. tuberculosis. Here we identify FipA as an interacting partner of FtsZ and FtsQ and establish that PknA-dependent phosphorylation of FipA on T77 and FtsZ on T343 is required for cell division under oxidative stress. A fipA knockout strain of M. smegmatis is less capable of withstanding oxidative stress than the wild type and showed elongation of cells due to a defect in septum formation. Localization of FtsQ, FtsZ and FipA at mid-cell was also compromised. Growth and survival defects under oxidative stress could be functionally complemented by fipA of M. tuberculosis but not its T77A mutant. Merodiploid strains of M. smegmatis expressing the FtsZ(T343A) showed inhibition of FtsZ-FipA interaction and Z ring formation under oxidative stress. Knockdown of FipA led to elongation of M. tuberculosis cells grown in macrophages and reduced intramacrophage growth. These data reveal a novel role of phosphorylation-dependent protein-protein interactions involving FipA, in the sustenance of mycobacterial cell division under oxidative stress.

Citation: Sureka K, Hossain T, Mukherjee P, Chatterjee P, Datta P, et al. (2010) Novel Role of

Contents 1 Protein Sequence 2 Human Homologue Blast Result 3 Alergen Protein 4 Bacterial Toxin Prediction 5 Subcellular Location 6 Antigens 6.1 B cell Epitopes 6.1.1 BCEpred Analysis 6.1.2 ABCpred Analysis 6.1.3 IEDB Analysis 7 MHC Class-I Binder 7.1 nHLAPred Analysis 7.2 IEDB Analysis 8 MHC Class-II Binder 8.1 Propred Analysis 8.2 NetMHC-II Analysis

Protein Sequence

>Rv0016c, TB.seq 18762:20234 MW:51577 MNASLRRISVTVMALIVLLLLNATMTQVFTADGLRADPRNQRVLLDEYSRQRGQITAGGQLLAYSVATDGRFRFLRVYPN PEVYAPVTGFYSLRYSSTALERAEDPILNGSDRRLFGRRLADFFTGRDPRGGNVDTTINPRIQQAGWDAMQQGCYGPCKG AVVALEPSTGKILALVSSPSYDPNLLASHNPEVQAQAWQRLGDNPASPLTNRAISETYPPGSTFKVITTAAALAAGATET EQLTAAPTIPLPGSTAQLENYGGAPCGDEPTVSLREAFVKSCNTAFVQLGIRTGADALRSMARAFGLDSPPRPTPLQVAE STVGPIPDSAALGMTSIGQKDVALTPLANAEIAATIANGGITMRPYLVGSLKGPDLANISTTVGYQQRRAVSPQVAAKLT ELMVGAEKVAQQKGAIPGVQIASKTGTAEHGTDPRHTPPHAWYIAFAPAQAPKVAVAVLVENGADRLSATGGALAAPIGR AVIEAALQGEP

Human Homologue Blast Result

subject ids	% identity	% positives	alignment length	evalue
sp|O75533	32	46	96	0.013
sp|Q8NBJ5	50	64	28	5.5
sp|P56715	24	42	142	6.5
sp|P98168	55	65	20	7.7
sp|A5PL33	31	42	61	9.7

Alergen Protein

Link to Algpred
Non Allergen Predicted by AlgPred Server

Bacterial Toxin Prediction

Link to btxpred
No Hit Fountd by btxpred server.

Subcellular Location

Link to TBpred
INTEGRAL MEMBRANE PROTEIN

Antigens

No Hit Found in AntigenDB
No. Hit Found in IEDB

B cell Epitopes

BCEpred Analysis

Link to Bcepred
Result Predicited by Bcepred

ABCpred Analysis

Link to ABCpred
Result Predicited by ABCPred

IEDB Analysis

Link to IEDB
Result Predicited by IEDB

MHC Class-I Binder

nHLAPred Analysis

Link to nHLApred
Result Predicited by [1]

IEDB Analysis

Link to IEDB
Result Predicted by [2]

MHC Class-II Binder

Propred Analysis

Link to Propred
Result Predicted by [3]

NetMHC-II Analysis

Link to NetMHC-II
Result Predicted by [4]