STF0_MYCTU
ID STF0_MYCTU Reviewed; 267 AA.
AC O53699; F2GM99; I6Y7G4; Q7DA29;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Trehalose 2-sulfotransferase {ECO:0000305|PubMed:15258569};
DE EC=2.8.2.37 {ECO:0000269|PubMed:15258569};
GN Name=stf0 {ECO:0000303|PubMed:15258569};
GN OrderedLocusNames=Rv0295c {ECO:0000312|EMBL:CCP43025.1},
GN LH57_01610 {ECO:0000312|EMBL:AIR13018.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27294 / TMC 102 / H37Rv;
RA Hazbon M.H., Riojas M.A., Damon A.M., Alalade R.O., Cantwell B.J.,
RA Monaco A., King S., Sohrabi A.;
RT "Phylogenetic analysis of Mycobacterial species using whole genome
RT sequences.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RC STRAIN=H37Rv;
RX PubMed=15258569; DOI=10.1038/nsmb802;
RA Mougous J.D., Petzold C.J., Senaratne R.H., Lee D.H., Akey D.L., Lin F.L.,
RA Munchel S.E., Pratt M.R., Riley L.W., Leary J.A., Berger J.M.,
RA Bertozzi C.R.;
RT "Identification, function and structure of the mycobacterial
RT sulfotransferase that initiates sulfolipid-1 biosynthesis.";
RL Nat. Struct. Mol. Biol. 11:721-729(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Catalyzes the sulfuryl group transfer from 3'-
CC phosphoadenosine-5'-phosphosulfate (PAPS) to trehalose, leading to
CC trehalose-2-sulfate (T2S). The sulfation of trehalose is the first step
CC in the biosynthesis of sulfolipid-1 (SL-1), a major cell wall
CC glycolipid and the most abundant sulfated metabolite found in
CC Mycobacterium tuberculosis, that is a potential virulence factor
CC thought to mediate host-pathogen interactions.
CC {ECO:0000269|PubMed:15258569}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + alpha,alpha-trehalose = 2-O-
CC sulfo-alpha,alpha-trehalose + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:41608, ChEBI:CHEBI:15378, ChEBI:CHEBI:16551,
CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:60091; EC=2.8.2.37;
CC Evidence={ECO:0000269|PubMed:15258569};
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:15258569}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0QQ53}.
CC -!- DISRUPTION PHENOTYPE: Loss of T2S and SL-1 formation. Unsulfated
CC acylated precursors of SL-1 are not detected, which indicates that Stf0
CC acts before lipid addition to trehalose. {ECO:0000269|PubMed:15258569}.
CC -!- SIMILARITY: Belongs to the Stf0 sulfotransferase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP43025.1; -; Genomic_DNA.
DR EMBL; CP009480; AIR13018.1; -; Genomic_DNA.
DR RefSeq; NP_214809.1; NC_000962.3.
DR RefSeq; WP_003401540.1; NZ_NVQJ01000026.1.
DR AlphaFoldDB; O53699; -.
DR SMR; O53699; -.
DR STRING; 83332.Rv0295c; -.
DR PaxDb; O53699; -.
DR PRIDE; O53699; -.
DR DNASU; 886596; -.
DR GeneID; 45424269; -.
DR GeneID; 886596; -.
DR KEGG; mtu:Rv0295c; -.
DR PATRIC; fig|83332.111.peg.331; -.
DR TubercuList; Rv0295c; -.
DR eggNOG; COG4424; Bacteria.
DR HOGENOM; CLU_098614_0_0_11; -.
DR OMA; QEEGWRN; -.
DR PhylomeDB; O53699; -.
DR BioCyc; MetaCyc:G185E-4418-MON; -.
DR BRENDA; 2.8.2.37; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0050656; F:3'-phosphoadenosine 5'-phosphosulfate binding; IDA:MTBBASE.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:MTBBASE.
DR GO; GO:0008146; F:sulfotransferase activity; IDA:MTBBASE.
DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:MTBBASE.
DR GO; GO:0046506; P:sulfolipid biosynthetic process; IDA:MTBBASE.
DR GO; GO:0005991; P:trehalose metabolic process; IDA:MTBBASE.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015124; Stf0.
DR InterPro; IPR024628; Sulfotransferase_Stf0_dom.
DR Pfam; PF09037; Sulphotransf; 1.
DR PIRSF; PIRSF021497; Sulphotransferase_Stf0; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Reference proteome; Transferase.
FT CHAIN 1..267
FT /note="Trehalose 2-sulfotransferase"
FT /id="PRO_0000434782"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:A0QQ53"
FT BINDING 14
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000250|UniProtKB:A0QQ53"
FT BINDING 33..39
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000250|UniProtKB:A0QQ53"
FT BINDING 48
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000250|UniProtKB:A0QQ53"
FT BINDING 53
FT /ligand="alpha,alpha-trehalose"
FT /ligand_id="ChEBI:CHEBI:16551"
FT /evidence="ECO:0000250|UniProtKB:A0QQ53"
SQ SEQUENCE 267 AA; 29775 MW; E60286DC61C5267C CRC64;
MSRAVRPYLV LATQRSGSTL LVESLRATGC AGEPQEFFQY LPSTGMAPQP REWFAGVDDD
TILQLLDPLD PGTPDTATPV AWREHVRTSG RTPNGVWGGK LMWNQTALLQ QRAAQLPDRS
GDGLRAAIRD VIGNEPVFVH VHRPDVVSQA VSFWRAVQTQ VWRGHPDPKR DSQAVYHAGA
IAHIIRNLRD QENGWRAWFA EEGIDPIDIA YPVLWRNLTA IVASVLDAIG QDPKLAPAPM
LERQANQRSD EWVDRYRAEA PRLGLPT
