Quick Search

Enter gene name or accession number


Search term: kdpD

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
Imagemap from R
To navigate upstream or downstream, click on the first or last gene

General annotation
Gene namekdpD
Rv numberRv1028c
TypeCDS
FunctionMember of the two-component regulatory system KDPD/KDPE involved in the regulation of the KDP operon. KDPD may function as a membrane-associated protein kinase that phosphorylates KDPE|Rv1027c in response to environmental signals.
ProductProbable sensor protein KdpD
CommentsRv1028c, (MTCY10G2.21), len: 860 aa. Probable kdpD, sensor protein, similar to others e.g. KDPD_ECOLI|P21865 sensor protein from Escherichia coli strain K12 (894 aa), FASTA scores: opt: 1041, E(): 0, (32.3% identity in 888 aa overlap); etc. Contains PS00017 ATP/GTP-binding site motif A (P-loop). Belongs to universal stress protein family.
Molecular mass (Da)92717.1
Isoelectric point5.8534
Gene length (bp)2583
Protein length860
Location (kb)1149.1


Functional categoryregulatory proteins


ProteomicsIdentified in the cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003). Required for growth in C57BL/6J mouse spleen, by transposon site hybridization (TraSH) in H37Rv (See Sassetti and Rubin, 2003). Non-essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). M. tuberculosis H37Rv kpdDE mutant shows increased virulence in SCID mice (See Parish et al., 2004).
see TB knockouts/mutants availability


Coordinates
TypeStartEndOrientation
CDS11491041151686-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1028c|kdpD
VTLLFADLCAIFTPYRWMIEHVTTKRGQLRIYLGAAPGVGKTYAMLGEAHRRLERGTDVV
AAVVETHGRNKTAKLLEGIEMIPPRYVEYRGARFPELDVEAVLRRHPQVVLVDELAHTNT
PGSKNPKRWQDVQEILDAGITVISTVNIQHLEGLNDVVEQITGIEQKEKIPDEIVRAADQ
VELVDITPEALRRRLAHGNVYAAERVDAALSNYFRTGNLTALREIALLWLADQVDAALEK
YRADKKITATWEARERVVVAVTGGPESETLVRRASRIASKSSAELMVVHVIRGDGLAGVS
APQLGRVRELATSLGATMHTVVGDDVPTALLDFAREMNATQLVVGTSRRSRWARLFDEGI
GARTVQEPGGIDVHMVTHPAASRASGWSRVSPRERHIASWLAALVVPSVICAITVAWLDR
FMGIGGESALFFIGVLIVALLGGVAPAALSALLSGMLLNYFLTEPRYTWTIAEPDAAVTE
FVLLAMAVAVAVLVDGAASRTREARRASQEAELLALFAGSVLRGADLATLLQRVRETYSQ
RAVTMLRVRQGASTGETVACVGTNPCRDVDSADTAIEVGDDEFWMLMAGRKLAARDRRVL
TAVATQAAGLVKQRELAEEAGQAEAIARADELRRSLLSAVSHDLRTPLAAAKVAVSSLRT
EDVAFSPEDTAELLATIEESIDQLTALVANLLDSSRLAAGVIRPQLRRAYLEEAVQRALV
SIGKGATGFYRSGIDRVKVDVGDAVAMADAGLLERVLANLIDNALRYAPDCVVRVNAGRV
RERVLINVIDEGPGVPRGTEEQLFAPFQRPGDHDNTTGVGLGMSVARGFVEAMGGTISAT
DTPGGGLTVVIDLAAPEDRP
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
Protein Data BankNo structure available
PFAMP96372


Orthologs/Cross-references
CDC1551MT1057
Enzyme Classification2.7.13.3
Gene Ontologytwo-component sensor activity
two-component signal transduction system (phosphorelay)
ATP binding
plasma membrane
response to stress
signal transduction
integral to membrane
peptidyl-histidine phosphorylation
M. bovisMb1056c
M. marinumMMAR_0634
M. smegmatisMSMEG_5395
UniProtP96372
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv1028c


Expression Data
TBDBRv1028c


Bibliography
Parish T, Smith DA, Kendall S, Casali N, Bancroft GJ, Stoker NG,
Deletion of two-component regulatory systems increases the virulence of Mycobacterium tuberculosis.
Infect Immun (2003) 71(3):1134-40
Cited for: Mutant/Secondary/Function
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Lamichhane G, Zignol M, Blades NJ, Geiman DE, Dougherty A, Grosset J, Broman KW, Bishai WR,
A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis.
Proc Natl Acad Sci U S A (2003) 100(12):7213-8
Cited for: Mutant
Sassetti CM, Rubin EJ,
Genetic requirements for mycobacterial survival during infection.
Proc Natl Acad Sci U S A (2003) 100(22):12989-94
Cited for: Mutant
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Hingley-Wilson SM, Lougheed KE, Ferguson K, Leiva S, Williams HD,
Individual Mycobacterium tuberculosis universal stress protein homologues are dispensable in vitro.
Tuberculosis (Edinb) (2010) 90(4):236-44
Cited for: Homology
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant