secG
- Type
- protein_coding
- Name
- secG
- Locus Name
-
Rv1440
- Product
-
Probable protein-export membrane protein (translocase subunit) SecG
- Functional Category
-
Cell wall and cell processes
- Location
- 1617837..1618070 (+ strand)
- Gene Length
- 233 bp
- Nucleotides
-
TGGAATTGGCCCTGCAGATCACGCTGATCGTCACGAGCGTGCTGGTGGTGTTGTTAGTACTGCTGCACCGGGCCAAGGGTGGCGGGCTATCGACACTGTTCGGCGGTGGTGTGCAGTCAAGCCTGTCCGGCTCGACGGTGGTGGAGAAGAACCTGGACCGGTTGACGCTGTTCGTTACCGGCATCTGGCTGGTGTCCATCATCGGCGTGGCGTTGCTCATCAAATACCGCTAG
- Drug Resistance
- Mutations
- Function
- Involved in protein export. Participates in an early event of protein translocation (By similarity). {ECO:0000250}.
- Family
-
SecG family
- GO
-
- protein secretion GO:0009306 biological_process
- P-P-bond-hydrolysis-driven protein transmembrane transporter activity GO:0015450 molecular_function
- plasma membrane GO:0005886 cellular_component
- evasion or tolerance by symbiont of host-produced reactive oxygen species GO:0052059 biological_process
- integral component of membrane GO:0016021 cellular_component
- InterPro
- Name
- Probable protein-export membrane protein SecG
- Family
- SecG family
- Protein Sequence
-
MELALQITLIVTSVLVVLLVLLHRAKGGGLSTLFGGGVQSSLSGSTVVEKNLDRLTLFVTGIWLVSIIGVALLIKYR
- Mass
- 8,163 Da
- Length
- 77 Aa
Rv1440 doesn't seem to be a targeted by any drug.
-
-
Tolerance of reactive oxygen produced by macrophages R-HSA-1222387
Homo sapiensR-HSA-1222387
-
-
-
Bacterial secretion system mtu03070
mtu03070Environmental Information Processing; Membrane transport
-
-
-
Protein export mtu03060
mtu03060Genetic Information Processing; Folding, sorting and degradation
-
-
-
Quorum sensing mtu02024
mtu02024Cellular Processes; Cellular community - prokaryotes
-
- 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.
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
- Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.