Rv2228c
- Type
- protein_coding
- Name
- Rv2228c
- Locus Name
-
Rv2228c
- Product
-
Multifunctional protein. Has RNASE H,alpha-ribazole phosphatase, and acid phosphatase activities.
- Functional Category
-
Information pathways
- Location
- 2501644..2502738 (- strand)
- Gene Length
- 1094 bp
- Nucleotides
-
GTGAAAGTTGTCATCGAAGCCGACGGCGGATCGCGGGGCAATCCCGGACCGGCCGGATACGGCGCGGTGGTGTGGACCGCCGATCACTCCACCGTGCTGGCCGAGTCCAAGCAGGCGATCGGCCGGGCGACGAACAACGTCGCCGAATACCGCGGCCTGATAGCCGGTTTGGACGACGCCGTGAAACTAGGTGCCACCGAGGCCGCGGTGCTGATGGACTCCAAGCTGGTGGTGGAGCAGATGTCCGGGCGGTGGAAGGTCAAGCACCCGGATCTGCTGAAGCTCTATGTCCAGGCTCAGGCGTTGGCGTCCCAGTTTCGCAGGATCAACTACGAGTGGGTTCCGCGTGCCCGGAACACGTATGCAGACCGGTTGGCCAATGACGCGATGGACGCCGCCGCGCAATCGGCTGCGGCGGATGCGGATCCTGCCAAAATCGTTGCGACCGAGTCACCGACATCTCCCGGCTGGACCGGCGCCCGCGGTACACCCACCCGACTACTTTTGTTGCGCCACGGGCAGACGGAGCTGTCGGAGCAACGCCGCTATTCGGGGCGCGGCAACCCGGGGTTGAACGAGGTGGGGTGGCGCCAGGTTGGTGCGGCGGCCGGGTATCTGGCGCGGCGCGGCGGGATCGCTGCGGTGGTCTCCTCGCCGCTACAGCGGGCTTACGACACCGCGGTGACCGCCGCCAGAGCCCTGGCCCTGGACGTGGTCGTCGATGACGACCTGGTCGAGACCGACTTCGGCGCCTGGGAGGGGCTGACGTTCGCGGAGGCCGCAGAACGCGATCCCGAGCTGCACCGTCGCTGGCTGCAGGACACCAGCATCACGCCCCCGGGTGGGGAAAGCTTCGACGACGTGCTGCGGCGGGTTCGGCGGGGACGTGATCGGATCATCGTTGGCTACGAAGGCGCGACGGTGCTGGTGGTGTCACATGTCACGCCGATCAAAATGTTGTTGCGGCTGGCGTTGGATGCCGGGTCGGGCGTCCTATATCGGTTGCATCTTGATCTGGCATCGCTGAGCATCGCCGAGTTCTACGCCGATGGGGCATCGTCGGTGCGATTGGTGAATCAGACAGGCTATCTATA
- Drug Resistance
- Mutations
- Function
- Endonuclease that displays both RNase H activity with a hybrid RNA/DNA substrate as well as double-stranded RNase activity. As the only authenticated RNase HI in M.tuberculosis, probably plays an important role in the physiology of this organism, being likely involved in bacterial replication. {ECO:0000269|PubMed:20363939}.; FUNCTION: Catalyzes the hydrolysis of the phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole (PubMed:20363939). May also catalyze the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12) (By similarity). Has a possible role in B12 recycling, but the primary role of the C-terminal domain of this phosphatase enzyme could be phosphate generation to help bacterial survival within the macrophage, which is a phosphate-deprived environment (PubMed:20363939). {ECO:0000250|UniProtKB:P39701, ECO:0000269|PubMed:20363939}.
- Family
-
RNase H family; Histidine phosphatase superfamily
- GO
-
- double-stranded RNA-specific ribonuclease activity GO:0032296 molecular_function
- metal ion binding GO:0046872 molecular_function
- DNA/RNA hybrid binding GO:0071667 molecular_function
- cobalamin biosynthetic process GO:0009236 biological_process
- RNA catabolic process GO:0006401 biological_process
- RNA-DNA hybrid ribonuclease activity GO:0004523 molecular_function
- alpha-ribazole phosphatase activity GO:0043755 molecular_function
- InterPro
3HST
- Name
- Bifunctional protein Rv2228c [Includes: Ribonuclease H (EC 3.1.26.4); Adenosylcobalamin/alpha-ribazole phosphatase (EC 3.1.3.73)]
- Family
- RNase H family; Histidine phosphatase superfamily
- Protein Sequence
-
MKVVIEADGGSRGNPGPAGYGAVVWTADHSTVLAESKQAIGRATNNVAEYRGLIAGLDDAVKLGATEAAVLMDSKLVVEQMSGRWKVKHPDLLKLYVQAQALASQFRRINYEWVPRARNTYADRLANDAMDAAAQSAAADADPAKIVATESPTSPGWTGARGTPTRLLLLRHGQTELSEQRRYSGRGNPGLNEVGWRQVGAAAGYLARRGGIAAVVSSPLQRAYDTAVTAARALALDVVVDDDLVETDFGAWEGLTFAEAAERDPELHRRWLQDTSITPPGGESFDDVLRRVRRGRDRIIVGYEGATVLVVSHVTPIKMLLRLALDAGSGVLYRLHLDLASLSIAEFYADGASSVRLVNQTGYL
- Mass
- 39,145 Da
- Length
- 364 Aa
Summary
Rv2228c doesn't seem to be a targeted by any drug.
-
-
DNA replication mtu03030
mtu03030Genetic Information Processing; Replication and repair
-
-
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Porphyrin and chlorophyll metabolism mtu00860
mtu00860PATHWAY_MAP mtu00860 Porphyrin and chlorophyll metabolism
-
- Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.
- J Bacteriol. 2010 Jun;192(11):2878-86. doi: 10.1128/JB.01615-09. Epub 2010 Apr 2.
- Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
- Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
- Cloning, expression, purification and preliminary crystallographic analysis of the RNase HI domain of the Mycobacterium tuberculosis protein Rv2228c as a maltose-binding protein fusion.
- Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):746-9. doi: 10.1107/S1744309108021118. Epub 2008 Jul 31.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.