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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 an undetermined metal cation with the hydrolysis of ATP [catalytic activity: ATP + H(2)O + undetermined metal cation(in) = ADP + phosphate + undetermined metal cation(out)].
ProductProbable metal cation transporter P-type ATPase CtpV
CommentsRv0969, (MTCY10D7.05c), len: 770 aa. Probable ctpV, metal cation transporter P-type ATPase (transmembrane protein) (see citation below), part of cso operon, highly similar (except in N-terminus) to others e.g. NP_391230.1|NC_000964 similar to heavy metal-transporting ATPase from Bacillus subtilis (803 aa); P37279|ATCS_SYNP7|PACS cation-transporting ATPase from Synechococcus sp. strain PCC 7942 (Anacystis nidulans R2) (747 aa), FASTA scores: opt: 1851, E(): 0, (52.1% identity in 664 aa overlap); etc. Equivalent to AAK45246.1 from Mycobacterium tuberculosis strain CDC1551 (792 aa) but shorter 22 aa. Contains PS00154 E1-E2 ATPases phosphorylation site. Belongs to the cation transport ATPases family (E1-E2 ATPases).
Functional categoryCell wall and cell processes
ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS; predicted transmembrane protein (See Gu et al., 2003). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS; predicted integral membrane protein (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 M. tuberculosis H37Rv-infected guinea pig lungs at 30 and 90 days (See Kruh 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).
TranscriptomicsmRNA identified by SCOTS method, 48h after infection of cultured human primary macrophages (see citation below). DNA 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). Expression in vtiro is increased in the presence of Cu and Ag, measured by qRT-PCR (See Ward et al., 2008).
OperonRv0968 and Rv0969, Rv0969 and Rv0970 are co-transcribed, by RT-PCR (See Liu et al., 2007).
MutantNon-essential gene 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). Non essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS10787431081055+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0969|ctpV
MRVCVTGFNVDAVRAVAIEETVSQVTGVHAVHAYPRTASVVIWYSPELGDTAAVLSAITKAQHVPAELVPARAPHSAGVRGVGVVRKITGGIRRMLSRPPGVDKPLKASRCGGRPRGPVRGSASWPGEQNRRERRTWLPRVWLALPLGLLALGSSMFFGAYPWAGWLAFAATLPVQFVAGWPILRGAVQQARALTSNMDTLIALGTLTAFVYSTYQLFAGGPLFFDTSALIIAFVVLGRHLEARATGKASEAISKLLELGAKEATLLVDGQELLVPVDQVQVGDLVRVRPGEKIPVDGEVTDGRAAVDESMLTGESVPVEKTAGDRVAGATVNLDGLLTVRATAVGADTALAQIVRLVEQAQGDKAPVQRLADRVSAVFVPAVIGVAVATFAGWTLIAANPVAGMTAAVAVLIIACPCALGLATPTAIMVGTGRGAELGILVKGGEVLEASKKIDTVVFDKTGTLTRARMRVTDVIAGQRRQPDQVLRLAAAVESGSEHPIGAAIVAAAHERGLAIPAANAFTAVAGHGVRAQVNGGPVVVGRRKLVDEQHLVLPDHLAAAAVEQEERGRTAVFVGQDGQVVGVLAVADTVKDDAADVVGRLHAMGLQVAMITGDNARTAAAIAKQVGIEKVLAEVLPQDKVAEVRRLQDQGRVVAMVGDGVNDAPALVQADLGIAIGTGTDVAIEASDITLMSGRLDGVVRAIELSRQTLRTIYQNLGWAFGYNTAAIPLAALGALNPVVAGAAMGFSSVSVVTNSLRLRRFGRDGRTA
      
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