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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionMetal cation-transporting ATPase; possibly catalyzes the transport of undetermined metal cation with the hydrolyse of ATP [catalytic activity: ATP + H(2)O + undetermined metal cation(in) = ADP + phosphate + undetermined metal cation(out)].
ProductProbable metal cation-transporting P-type ATPase C CtpC
CommentsRv3270, (MT3370, MTCY71.10), len: 718 aa. Probable ctpC, metal cation-transport ATPase P-type, integral membrane protein, equivalent to Q9CCL1|CTPC|ML0747 putative cation transport ATPase from Mycobacterium leprae (725 aa), FASTA scores: opt: 3908, E(): 0, (85.95% identity in 713 aa overlap). Also similar to O66027|MTAA metal transporting ATPase MTA72 from Mycobacterium tuberculosis (680 aa), FASTA scores: opt: 3756, E(): 5.5e-213, (91.45% identity in 679 aa overlap); and to other ATPases e.g. Q9ZHC7|SILP_SALTY putative cation transporting P-type ATPase from Salmonella typhimurium (824 aa), FASTA scores: opt: 1145, E(): 1.3e-59, (36.55% identity in 643 aa overlap); Q9HX93|PA3920 probable metal transporting P-type ATPase from Pseudomonas aeruginosa (792 aa), FASTA scores: opt: 1140, E(): 2.4e-59, (35.95% identity in 745 aa overlap); etc. Contains PS00154 E1-E2 ATPases phosphorylation site. Belongs to the cation transport ATPases family (E1-E2 ATPases), subfamily IB.
Functional categoryCell wall and cell processes
ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011).
TranscriptomicsDNA microarrays detect expression in M. tuberculosis H37Rv in vivo (in BALB/c and SCID mice) but not in vitro (in 7H9 medium) (See Talaat et al., 2004).
MutantEssential gene (growth defect) for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Required for growth in C57BL/6J mouse spleen, by transposon site hybridization (TraSH) in H37Rv (See Sassetti and Rubin, 2003).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS36505263652682+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3270|ctpC
MTLEVVSDAAGRMRVKVDWVRCDSRRAVAVEEAVAKQNGVRVVHAYPRTGSVVVWYSPRRADRAAVLAAIKGAAHVAAELIPARAPHSAEIRNTDVLRMVIGGVALALLGVRRYVFARPPLLGTTGRTVATGVTIFTGYPFLRGALRSLRSGKAGTDALVSAATVASLILRENVVALTVLWLLNIGEYLQDLTLRRTRRAISELLRGNQDTAWVRLTDPSAGSDAATEIQVPIDTVQIGDEVVVHEHVAIPVDGEVVDGEAIVNQSAITGENLPVSVVVGTRVHAGSVVVRGRVVVRAHAVGNQTTIGRIISRVEEAQLDRAPIQTVGENFSRRFVPTSFIVSAIALLITGDVRRAMTMLLIACPCAVGLSTPTAISAAIGNGARRGILIKGGSHLEQAGRVDAIVFDKTGTLTVGRPVVTNIVAMHKDWEPEQVLAYAASSEIHSRHPLAEAVIRSTEERRISIPPHEECEVLVGLGMRTWADGRTLLLGSPSLLRAEKVRVSKKASEWVDKLRRQAETPLLLAVDGTLVGLISLRDEVRPEAAQVLTKLRANGIRRIVMLTGDHPEIAQVVADELGIDEWRAEVMPEDKLAAVRELQDDGYVVGMVGDGINDAPALAAADIGIAMGLAGTDVAVETADVALANDDLHRLLDVGDLGERAVDVIRQNYGMSIAVNAAGLLIGAGGALSPVLAAILHNASSVAVVANSSRLIRYRLDR