STAL_STRTO
ID STAL_STRTO Reviewed; 270 AA.
AC Q8KLM3;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Desulfo-A47934 sulfotransferase {ECO:0000305};
DE EC=2.8.2.36 {ECO:0000269|PubMed:16492565};
GN Name=staL {ECO:0000303|PubMed:12060705};
GN ORFNames=BU52_01305 {ECO:0000312|EMBL:KES08714.1};
OS Streptomyces toyocaensis.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=55952;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRRL 15009;
RX PubMed=9177243; DOI=10.1073/pnas.94.12.6480;
RA Marshall C.G., Broadhead G., Leskiw B.K., Wright G.D.;
RT "D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are
RT highly homologous to the enterococcal vancomycin-resistance ligases VanA
RT and VanB.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6480-6483(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NRRL 15009;
RX PubMed=12060705; DOI=10.1073/pnas.102285099;
RA Pootoolal J., Thomas M.G., Marshall C.G., Neu J.M., Hubbard B.K.,
RA Walsh C.T., Wright G.D.;
RT "Assembling the glycopeptide antibiotic scaffold: the biosynthesis of
RT A47934 from Streptomyces toyocaensis NRRL15009.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:8962-8967(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 15009;
RA Hong H.-J., Kwun M.J.;
RT "The genome announcement of Streptomyces toyocaensis NRRL15009.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=16492565; DOI=10.1016/j.chembiol.2005.12.003;
RA Lamb S.S., Patel T., Koteva K.P., Wright G.D.;
RT "Biosynthesis of sulfated glycopeptide antibiotics by using the
RT sulfotransferase StaL.";
RL Chem. Biol. 13:171-181(2006).
RN [5] {ECO:0007744|PDB:2OV8, ECO:0007744|PDB:2OVB, ECO:0007744|PDB:2OVF}
RP X-RAY CRYSTALLOGRAPHY (2.58 ANGSTROMS) OF 4-270 IN COMPLEX WITH ADENOSINE
RP 3',5'-BISPHOSPHATE (PAP), SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF TRP-34;
RP HIS-43; PHE-77; SER-98; ARG-101; TRP-132; ARG-202; GLU-205 AND GLU-206.
RX PubMed=17329243; DOI=10.1074/jbc.m611912200;
RA Shi R., Lamb S.S., Bhat S., Sulea T., Wright G.D., Matte A., Cygler M.;
RT "Crystal structure of StaL, a glycopeptide antibiotic sulfotransferase from
RT Streptomyces toyocaensis.";
RL J. Biol. Chem. 282:13073-13086(2007).
RN [6] {ECO:0007744|PDB:4EEC}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 4-270 IN COMPLEX WITH ADENOSINE
RP 3',5'-BISPHOSPHATE (PAP) AND DESULFO-A47934 (DSA), AND SUBUNIT.
RX PubMed=22753479; DOI=10.1073/pnas.1205377109;
RA Shi R., Munger C., Kalan L., Sulea T., Wright G.D., Cygler M.;
RT "Sulfonation of glycopeptide antibiotics by sulfotransferase StaL depends
RT on conformational flexibility of aglycone scaffold.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11824-11829(2012).
CC -!- FUNCTION: Catalyzes the sulfonation of desulfo-A47934, the final step
CC of A47934 biosynthesis. Has also weak activity in vitro with
CC teicoplanin aglycone and teicoplanin. {ECO:0000269|PubMed:16492565}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + desulfo-A47934 = A47934 +
CC adenosine 3',5'-bisphosphate + H(+); Xref=Rhea:RHEA:40227,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:76892, ChEBI:CHEBI:76894; EC=2.8.2.36;
CC Evidence={ECO:0000269|PubMed:16492565};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000269|PubMed:16492565}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16492565,
CC ECO:0000269|PubMed:17329243, ECO:0000269|PubMed:22753479}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant produces desulfo-A47934 but not
CC A47934. {ECO:0000269|PubMed:16492565}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U82965; AAM80529.1; -; Genomic_DNA.
DR EMBL; JFCB01000001; KES08714.1; -; Genomic_DNA.
DR RefSeq; WP_037926427.1; NZ_JFCB01000001.1.
DR PDB; 2OV8; X-ray; 2.58 A; A=4-270.
DR PDB; 2OVB; X-ray; 2.61 A; A=4-270.
DR PDB; 2OVF; X-ray; 2.95 A; A=4-270.
DR PDB; 4EEC; X-ray; 2.70 A; A/B=4-270.
DR PDBsum; 2OV8; -.
DR PDBsum; 2OVB; -.
DR PDBsum; 2OVF; -.
DR PDBsum; 4EEC; -.
DR AlphaFoldDB; Q8KLM3; -.
DR SMR; Q8KLM3; -.
DR DIP; DIP-60053N; -.
DR STRING; 55952.BU52_01305; -.
DR EnsemblBacteria; KES08714; KES08714; BU52_01305.
DR KEGG; ag:AAM80529; -.
DR eggNOG; ENOG5032252; Bacteria.
DR BRENDA; 2.8.2.36; 6104.
DR EvolutionaryTrace; Q8KLM3; -.
DR Proteomes; UP000028341; Unassembled WGS sequence.
DR GO; GO:0008146; F:sulfotransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..270
FT /note="Desulfo-A47934 sulfotransferase"
FT /id="PRO_0000435393"
FT ACT_SITE 67
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P49891,
FT ECO:0000305|PubMed:17329243"
FT BINDING 12..17
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:17329243,
FT ECO:0000305|PubMed:22753479"
FT BINDING 43..46
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:22753479"
FT BINDING 90
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:17329243,
FT ECO:0000305|PubMed:22753479"
FT BINDING 98..101
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:17329243,
FT ECO:0000305|PubMed:22753479"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:22753479"
FT BINDING 163
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:17329243,
FT ECO:0000305|PubMed:22753479"
FT BINDING 196..198
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000305|PubMed:22753479"
FT MUTAGEN 34
FT /note="W->F: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 43
FT /note="H->A: 80% decrease in activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 77
FT /note="F->E: 90% decrease in activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 98
FT /note="S->A: 60% decrease in activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 101
FT /note="R->A: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 132
FT /note="W->F: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 202
FT /note="R->A: 15% decrease in activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 205
FT /note="E->A: Almost loss of activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT MUTAGEN 206
FT /note="E->A: 30% decrease in activity."
FT /evidence="ECO:0000269|PubMed:17329243"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 15..27
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 44..49
FT /evidence="ECO:0007829|PDB:2OV8"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:2OV8"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2OV8"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:2OV8"
FT TURN 111..115
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 116..123
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:2OV8"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2OV8"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:2OV8"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:2OV8"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2OV8"
FT HELIX 258..265
FT /evidence="ECO:0007829|PDB:2OV8"
SQ SEQUENCE 270 AA; 30172 MW; 1AA4D831B508327A CRC64;
MNGMCWIASY PKAGGHWLRC MLTSYVTGEP VETWPGIQAG VPHLEGLLRD GEAPSADPDE
QVLLATHFTA DRPVLRFYRE STAKVVCLIR NPRDAMLSLM RMKGIPPEDV EACRKIAETF
IADEGFSSVR IWAGEGSWPE NIRSWTDSVH ESFPNAAVLA VRYEDLRKDP EGELWKVVDF
LELGGRDGVA DAVANCTLER MREMEERSKL LGLETTGLMT RGGKQLPFVG KGGQRKSLKF
MGDDIEKAYA DLLHGETDFA HYARLYGYAE
