Rv0295c - conserved hypothetical protein

Expression: Most Significant Conditions for Rv0295c

Protein Domains

Gene Information
Locus	Rv0295c
Symbol
Gene Name	conserved hypothetical protein
Location	358945 - 359748 (-)
Species	Mycobacterium tuberculosis H37Rv complete genome.
Length	Gene:804 bp Protein:268 aa
External Links	Tuberculist Target Gene Information String Protein-Protein Interactions STITCH Chemical-Protein Interactions Search Google Scholar
Orthologs
Orthogroup Number	2807
Related Genes	MAP2118 MAV_2058 Mkms_0398 Mmcs_0389 MSMEG_0630 MT0308
Transcriptional Regulation
Operons	View gene in operon browser
Regulatory Network	Search for regulators of Rv0295c
Expression Correlation	Genes with Correlated Expression Scatterplot of Gene Expression

Sequence

Proteins

>Rv0295c Transcript 1
MSRAVRPYLVLATQRSGSTLLVESLRATGCAGEPQEFFQYLPSTGMAPQPREWFAGVDDD
TILQLLDPLDPGTPDTATPVAWREHVRTSGRTPNGVWGGKLMWNQTALLQQRAAQLPDRS
GDGLRAAIRDVIGNEPVFVHVHRPDVVSQAVSFWRAVQTQVWRGHPDPKRDSQAVYHAGA
IAHIIRNLRDQENGWRAWFAEEGIDPIDIAYPVLWRNLTAIVASVLDAIGQDPKLAPAPM
LERQANQRSDEWVDRYRAEAPRLGLPT*

Genomic Sequence

>Rv0295c
ATGTCCCGCGCTGTGAGACCGTATCTGGTGCTCGCCACCCAACGCAGCGGCAGCACGCTG
CTGGTGGAATCGCTGCGCGCGACGGGCTGTGCCGGGGAACCACAGGAGTTCTTCCAATAC
CTGCCTAGCACCGGGATGGCCCCCCAGCCCCGGGAGTGGTTCGCTGGGGTCGACGATGAC
ACGATCCTGCAATTGCTCGATCCGCTGGACCCCGGTACACCGGACACCGCGACGCCGGTT
GCCTGGCGTGAGCACGTCCGCACCTCCGGTCGCACGCCCAACGGCGTCTGGGGCGGCAAG
TTGATGTGGAATCAGACTGCGCTGCTGCAGCAACGCGCAGCACAATTGCCGGATCGCTCC
GGGGATGGCTTGCGCGCGGCAATCCGCGACGTCATTGGCAACGAACCGGTTTTCGTGCAC
GTCCACCGGCCCGATGTGGTGTCACAAGCGGTGTCGTTCTGGCGCGCCGTGCAAACCCAG
GTTTGGCGGGGCCATCCGGACCCCAAGCGCGACTCGCAGGCCGTCTACCACGCCGGTGCC
ATCGCCCACATCATCAGGAATCTGCGCGATCAGGAAAACGGCTGGCGCGCTTGGTTTGCC
GAGGAAGGCATCGATCCGATCGATATCGCCTACCCGGTGTTATGGCGCAACCTGACCGCG
ATTGTGGCCAGTGTGCTTGACGCCATCGGCCAGGATCCCAAACTGGCGCCCGCACCGATG
CTGGAACGGCAGGCCAACCAGCGCTCTGATGAGTGGGTCGACCGGTACCGAGCGGAGGCG
CCGCGGCTGGGGCTACCCACCTGA

Community Annotations Pending Curatorial Review

Field	Value	Status	Creator	Date
Term	TBRXN:TRESULT trehalose sulfotransferase - ISS	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Term	EC:2.8.2.2 Alcohol sulfotransferase. - ISS	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Term	TBRXN:TRESULT trehalose sulfotransferase - ISS	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Term	EC:2.8.2.2 Alcohol sulfotransferase. - ISS	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Term	TBRXN:TRESULT trehalose sulfotransferase - IDA	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Term	EC:2.8.2.2 Alcohol sulfotransferase. - IDA	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 CA. Rivera-Marrero, JD. Ritzenthaler et al. Molecular cloning and expression of a novel glycolipid sulfotransferase in Mycobacterium tuberculosis. Microbiology (Reading, Engl.) 2002
Term	TBRXN:TRESULT trehalose sulfotransferase - IDA	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Term	EC:2.8.2.2 Alcohol sulfotransferase. - IDA	active	njamshidi	2012-10-05
	PMID: 15258569 show biochemically that paps is the sulfate donor. see also PMID: 11882713 authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Name	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I	active	mjackson	2012-10-05
	Polymethyl-branched acyltrehaloses
Symbol	sft0	active	mjackson	2012-10-05
	Polymethyl-branched acyltrehaloses
Name	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I	active	mjackson	2012-10-05
	Polymethyl-branched acyltrehaloses
Symbol	sft0	active	mjackson	2012-10-05
	Polymethyl-branched acyltrehaloses
Other	TBPWY:Polymethyl-branched acyltrehaloses	active	mjackson	2012-03-05
	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic) authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004
Symbol	sft0	active	mjackson	2012-03-05
	Sulfotransferase responsible for the formation of the trehalose-2-sulfate moiety of sulfolipid-I (phenotypic [mycobacterial recombinant strains]; enzymatic) authors,JD. Mougous,CJ. Petzold,RH. Senaratne,DH. Lee,DL. Akey,FL. Lin,SE. Munchel,MR. Pratt,LW. Riley,JA. Leary,JM. Berger,CR. Bertozzi Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis. Nat. Struct. Mol. Biol. 2004