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Search term: Rv2916c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nameffh
Rv numberRv2916c
TypeCDS
FunctionNecessary for efficient export of extra-cytoplasmic proteins. Binds to the signal sequence when it emerges from the ribosomes.
ProductProbable signal recognition particle protein Ffh (fifty-four homolog) (SRP protein)
CommentsRv2916c, (MTCY338.04c), len: 525 aa. Probable ffh, signal recognition particle (SRP) protein (ala-, gly-, leu-rich protein) (see citation below), equivalent to O33013|SR54_MYCLE signal recognition particle from Mycobacterium leprae (521 aa), FASTA scores: opt: 2968, E(): 1.6e-145, (87.85% identity in 526 aa overlap). Also highly similar to others e.g. O69874|FFH from Streptomyces coelicolor (550 aa), FASTA scores: opt: 2025, E(): 6e-97, (63.8% identity in 519 aa overlap) (N-terminus longer 34 aa); P37105|SR54_BACSU from Bacillus subtilis (446 aa), FASTA scores: opt: 1451, E(): 1.9e-67, (51.5% identity in 435 aa overlap); BAB57399|FFH from Staphylococcus aureus subsp. aureus Mu50 (455 aa), FASTA scores: opt: 1418, E(): 9.4e-66, (48.65% identity in 448 aa overlap); etc. Contains PS00017 ATP/GTP-binding site motif A (P-loop). Belongs to the SRP family of GTP-binding proteins. Note that signal recognition particle consists of a small cytoplasmic RNA (SC-RNA) molecule and protein FFH. The protein has a two domain structure: the G-domain binds GTP; the M-domain binds the RNA and also binds the signal sequence.
Molecular mass (Da)54969.5
Isoelectric point8.4695
Gene length (bp)1578
Protein length525
Location (kb)3224.71


Functional categorycell wall and cell processes


ProteomicsIdentified in the cell wall and cell membrane fractions of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong 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). Translational start site supported by proteomics data (See Kelkar et al., 2011).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Coordinates
TypeStartEndOrientation
CDS32247083226285-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv2916c|ffh
VFESLSDRLTAALQGLRGKGRLTDADIDATTREIRLALLEADVSLPVVRAFIHRIKERAR
GAEVSSALNPAQQVVKIVNEELISILGGETRELAFAKTPPTVVMLAGLQGSGKTTLAGKL
AARLRGQGHTPLLVACDLQRPAAVNQLQVVGERAGVPVFAPHPGASPESGPGDPVAVAAA
GLAEARAKHFDVVIVDTAGRLGIDEELMAQAAAIRDAINPDEVLFVLDAMIGQDAVTTAA
AFGEGVGFTGVALTKLDGDARGGAALSVREVTGVPILFASTGEKLEDFDVFHPDRMASRI
LGMGDVLSLIEQAEQVFDAQQAEEAAAKIGAGELTLEDFLEQMLAVRKMGPIGNLLGMLP
GAAQMKDALAEVDDKQLDRVQAIIRGMTPQERADPKIINASRRLRIANGSGVTVSEVNQL
VERFFEARKMMSSMLGGMGIPGIGRKSATRKSKGAKGKSGKKSKKGTRGPTPPKVKSPFG
VPGMPGLAGLPGGLPDLSQMPKGLDELPPGLADFDLSKLKFPGKK
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
Protein Data BankNo structure available
PFAMP66844


Orthologs/Cross-references
CDC1551MT2984
Gene Ontologyprotein binding
GTP binding
signal recognition particle, endoplasmic reticulum targeting
SRP-dependent cotranslational protein targeting to membrane
7S RNA binding
nucleoside-triphosphatase activity
M. bovisMb2940c
M. lepraeML1622
M. marinumMMAR_1792
M. smegmatisMSMEG_2430
UniProtP66844
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv2916c


Expression Data
TBDBRv2916c


Bibliography
Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
Cited for: Mutant
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Xiong Y, Chalmers MJ, Gao FP, Cross TA, Marshall AG,
Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry.
J Proteome Res (2005) 4(3):855-61
Cited for: Proteomics
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant
Braunstein M, Belisle JT,
Molecular Genetics of Mycobacteria; Thirteenth chapter: Genetics of Protein Secretion
ASM Press (2000) 1-55581-191-4:203-220
Cited for: Review