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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
FunctionUnknown (could mediate bacterial attachment to host cells).
ProductAlanine and proline rich secreted protein Apa (fibronectin attachment protein) (immunogenic protein MPT32) (antigen MPT-32) (45-kDa glycoprotein) (45/47 kDa antigen)
CommentsRv1860, (MT1908, MTCY359.0013), len: 325 aa. Apa (alternate gene names: mpt32, modD), Ala-, Pro-rich 45/47 kDa secreted protein, very similar to P46842|N43L_MYCLE from Mycobacterium leprae (287 aa), FASTA scores: opt: 1166, E(): 0, (66.4% identity in 298 aa overlap). Known to be glycosylated fibronectin-binding protein (see some citations). Changes in the mannosylation pattern of this protein affect its ability to stimulate T-lymphocyte response. Major immunodominant antigen that has potential as a vaccine against tuberculosis. APA-ELISA could be used in diagnosis.
Functional categoryCell wall and cell processes
ProteomicsThe product of this CDS corresponds to spots 1860 identified in short term culture filtrate by proteomics at the Statens Serum Institute (Denmark) (see proteomics citations from 2000). Identified in immunodominant fractions of M. tuberculosis H37Rv culture filtrate using 2D-LPE, 2D-PAGE, and LC-MS or LC-MS/MS (See Covert et al., 2001). Also identified by proteomics during starvation as downregulated (see Betts et al., 2002). Identified in the culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Predicted secreted protein - identified in culture filtrates of M. tuberculosis H37Rv; signal peptide predicted (See Malen et al., 2007). Identified in the culture filtrate of M. tuberculosis H37Rv using LC-MS/MS; antigen recognized by serum pool from tuberculosis patients (See Malen et al., 2008). Putative glycoprotein identified by LC/ESI-MS/MS in the culture filtrate of M. tuberculosis H37Rv (See Gonzalez-Zamorano et al., 2009). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011).
TranscriptomicsmRNA identified by DNA microarray analysis and possibly down-regulated by hrcA|Rv2374c (see Stewart et al., 2002).
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
CDS21077362108713+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv1860|apa
MHQVDPNLTRRKGRLAALAIAAMASASLVTVAVPATANADPEPAPPVPTTAASPPSTAAAPPAPATPVAPPPPAAANTPNAQPGDPNAAPPPADPNAPPPPVIAPNAPQPVRIDNPVGGFSFALPAGWVESDAAHFDYGSALLSKTTGDPPFPGQPPPVANDTRIVLGRLDQKLYASAEATDSKAAARLGSDMGEFYMPYPGTRINQETVSLDANGVSGSASYYEVKFSDPSKPNGQIWTGVIGSPAANAPDAGPPQRWFVVWLGTANNPVDKGAAKALAESIRPLVAPPPAPAPAPAEPAPAPAPAGEVAPTPTTPTPQRTLPA
      
Bibliography