STF0_MYCTE
ID STF0_MYCTE Reviewed; 267 AA.
AC A0A0H3L952;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 2.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Trehalose 2-sulfotransferase {ECO:0000250|UniProtKB:O53699};
DE EC=2.8.2.37 {ECO:0000250|UniProtKB:O53699};
GN Name=stf0 {ECO:0000303|PubMed:22360425};
GN OrderedLocusNames=ERDMAN_0329 {ECO:0000312|EMBL:BAL64146.1};
OS Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=652616;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=22535945; DOI=10.1128/jb.00353-12;
RA Miyoshi-Akiyama T., Matsumura K., Iwai H., Funatogawa K., Kirikae T.;
RT "Complete annotated genome sequence of Mycobacterium tuberculosis Erdman.";
RL J. Bacteriol. 194:2770-2770(2012).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 35801 / TMC 107 / Erdman;
RX PubMed=22360425; DOI=10.1021/cb200311s;
RA Gilmore S.A., Schelle M.W., Holsclaw C.M., Leigh C.D., Jain M., Cox J.S.,
RA Leary J.A., Bertozzi C.R.;
RT "Sulfolipid-1 biosynthesis restricts Mycobacterium tuberculosis growth in
RT human macrophages.";
RL ACS Chem. Biol. 7:863-870(2012).
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:0000250|UniProtKB:O53699, ECO:0000269|PubMed:22360425}.
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:0000250|UniProtKB:O53699};
CC -!- PATHWAY: Glycolipid metabolism. {ECO:0000269|PubMed:22360425}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0QQ53}.
CC -!- DISRUPTION PHENOTYPE: Loss of T2S and SL-1 formation, but phthiocerol
CC dimycocerosate (PDIM) biosynthesis remains intact. Cells lacking this
CC gene exhibit augmented survival in human but not murine macrophages,
CC suggesting that SL-1 negatively regulates the intracellular growth of
CC M.tuberculosis in a species-specific manner. Moreover, the mutant
CC strains exhibit increased resistance in vitro to a human cationic
CC antimicrobial peptide, LL-37, while they do not show global defects in
CC overall cell envelope integrity. {ECO:0000269|PubMed:22360425}.
CC -!- SIMILARITY: Belongs to the Stf0 sulfotransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAL64146.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP012340; BAL64146.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003401540.1; NZ_KK339487.1.
DR AlphaFoldDB; A0A0H3L952; -.
DR SMR; A0A0H3L952; -.
DR EnsemblBacteria; BAL64146; BAL64146; ERDMAN_0329.
DR GeneID; 45424269; -.
DR KEGG; mtn:ERDMAN_0329; -.
DR PATRIC; fig|652616.3.peg.334; -.
DR HOGENOM; CLU_098614_0_0_11; -.
DR Proteomes; UP000007568; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Transferase.
FT CHAIN 1..267
FT /note="Trehalose 2-sulfotransferase"
FT /id="PRO_0000434784"
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
