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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
FunctionInvolved in protein export. May interact with the SECY/SECE subunits. SECA has a central role in coupling the hydrolysis of ATP to the transfer of PRE-secretory periplasmic and outer membrane proteins across the membrane.
ProductPossible preprotein translocase ATPase SecA2
CommentsRv1821, (MTCY1A11.22c), len: 808 aa. Possible secA2, preprotein translocase and ATPase, component of secretion apparatus (see Braunstein & Belisle 2000), similar to several preprotein translocases e.g. P28366|SECA_BACSU preprotein translocase secA subunit from Bacillus subtilis (841 aa), FASTA scores: opt: 1424, E(): 0, (35.9% identity in 786 aa overlap). Equivalent to AL008609|MLCB1788.45 Preprotein translocase SecA 2 from Mycobacterium leprae (778 aa) (87.1% identity in 780 aa overlap). Also similar to Rv3240c|MTCY20B11.15c secA preprotein translocase from Mycobacterium tuberculosis (949 aa). Could be part of the prokaryotic protein translocation apparatus which comprise SECA|Rv3240c, SECD|Rv2587c, SECE|Rv0638, SECF|Rv2586c, SECG|Rv1440 and SECY|Rv0732. Binds ATP.
Functional categoryCell wall and cell processes
ProteomicsIdentified by proteomics at the Statens Serum Institute (Denmark) (see Rosenkrands et al., 2000). Identified 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 by mass spectrometry in whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011).
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 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). Required for survival in primary murine macrophages, by transposon site hybridization (TraSH) in H37Rv (See Rengarajan et al., 2005). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). M. tuberculosis H37Rv secA2|Rv1821 mutant shows growth defect in C57BL/6 mice, and in unactivated bone marrow-derived macrophages from C57BL/6, p47 phox-/-, gp91phox-/-, and NOS2-/- mice; growth is comparable in activated macrophages from C57BL/6; C57BL/6 mice infected with mutant survive longer than with wild-type (See Kurtz et al., 2006). M. tuberculosis H37Rv secA2|Rv1821 mutant shows growth defect in C57BL/6 bone marrow-derived macrophages (See Hou et al., 2008; Rigel et al., 2009) that can not be complemented by secA2 with K115R mutation; K115R in the Walker A motif decreases ATP binding (See Hou et al., 2008). M. tuberculosis H37Rv secA2|Rv1821 mutant colony morpholgy is altered; wild-type M. tuberculosis expressing secA2 with K115R mutation has colony morphology similar to secA2 mutant (See Rigel et al., 2009).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS20664572068883+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv1821|secA2
VNVHGCPRIAACRCTDTHPRGRPAFAYRWFVPKTTRAQPGRLSSRFWRLLGASTEKNRSRSLADVTASAEYDKEAADLSDEKLRKAAGLLNLDDLAESADIPQFLAIAREAAERRTGLRPFDVQLLGALRMLAGDVIEMATGEGKTLAGAIAAAGYALAGRHVHVVTINDYLARRDAEWMGPLLDAMGLTVGWITADSTPDERRTAYDRDVTYASVNEIGFDVLRDQLVTDVNDLVSPNPDVALIDEADSVLVDEALVPLVLAGTTHRETPRLEIIRLVAELVGDKDADEYFATDSDNRNVHLTEHGARKVEKALGGIDLYSEEHVGTTLTEVNVALHAHVLLQRDVHYIVRDDAVHLINASRGRIAQLQRWPDGLQAAVEAKEGIETTETGEVLDTITVQALINRYATVCGMTGTALAAGEQLRQFYQLGVSPIPPNKPNIREDEADRVYITTAAKNDGIVEHITEVHQRGQPVLVGTRDVAESEELHERLVRRGVPAVVLNAKNDAEEARVIAEAGKYGAVTVSTQMAGRGTDIRLGGSDEADHDRVAELGGLHVVGTGRHHTERLDNQLRGRAGRQGDPGSSVFFSSWEDDVVAANLDHNKLPMATDENGRIVSPRTGSLLDHAQRVAEGRLLDVHANTWRYNQLIAQQRAIIVERRNTLLRTVTAREELAELAPKRYEELSDKVSEERLETICRQIMLYHLDRGWADHLAYLADIRESIHLRALGRQNPLDEFHRMAVDAFASLAADAIEAAQQTFETANVLDHEPGLDLSKLARPTSTWTYMVNDNPLSDDTLSALSLPGVFR
      
Bibliography