ISPT_STRPN
ID ISPT_STRPN Reviewed; 252 AA.
AC Q97SR4;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Isoprenyl transferase {ECO:0000255|HAMAP-Rule:MF_01139};
DE EC=2.5.1.- {ECO:0000255|HAMAP-Rule:MF_01139};
GN Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=SP_0261;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC with allylic pyrophosphates generating different type of terpenoids.
CC {ECO:0000255|HAMAP-Rule:MF_01139}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01139};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}.
CC -!- INTERACTION:
CC Q97SR4; P0A2W6: acpS; NbExp=2; IntAct=EBI-2206983, EBI-2207344;
CC Q97SR4; P63544: apt; NbExp=2; IntAct=EBI-2206983, EBI-2207316;
CC Q97SR4; P63588: aroD; NbExp=2; IntAct=EBI-2206983, EBI-2207290;
CC Q97SR4; P95830: dnaJ; NbExp=2; IntAct=EBI-2206983, EBI-2207079;
CC Q97SR4; Q97QS2: eno; NbExp=2; IntAct=EBI-2206983, EBI-2207206;
CC Q97SR4; Q97SE7: gatB; NbExp=2; IntAct=EBI-2206983, EBI-2207023;
CC Q97SR4; Q97SE5: gatC; NbExp=2; IntAct=EBI-2206983, EBI-2207053;
CC Q97SR4; Q97NV3: groES; NbExp=2; IntAct=EBI-2206983, EBI-2206949;
CC Q97SR4; Q97S73: grpE; NbExp=2; IntAct=EBI-2206983, EBI-2207065;
CC Q97SR4; P65144: infC; NbExp=2; IntAct=EBI-2206983, EBI-2207149;
CC Q97SR4; A0A0H2UNP1: lacF-1; NbExp=3; IntAct=EBI-2206983, EBI-2207447;
CC Q97SR4; P0A4T1: malR; NbExp=2; IntAct=EBI-2206983, EBI-2207435;
CC Q97SR4; P41354: mutX; NbExp=2; IntAct=EBI-2206983, EBI-2207232;
CC Q97SR4; P65887: purA; NbExp=2; IntAct=EBI-2206983, EBI-2206955;
CC Q97SR4; P0CB75: pyrF; NbExp=2; IntAct=EBI-2206983, EBI-2207109;
CC Q97SR4; P65946: pyrR; NbExp=2; IntAct=EBI-2206983, EBI-2207248;
CC Q97SR4; Q97QV8: rex; NbExp=2; IntAct=EBI-2206983, EBI-2207177;
CC Q97SR4; Q97NX6: scpB; NbExp=2; IntAct=EBI-2206983, EBI-2206697;
CC Q97SR4; A0A0H2UQ93: smc; NbExp=2; IntAct=EBI-2206983, EBI-6474424;
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_01139}.
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DR EMBL; AE005672; AAK74439.1; -; Genomic_DNA.
DR PIR; F95030; F95030.
DR RefSeq; WP_000466719.1; NZ_AKVY01000001.1.
DR PDB; 5KH2; X-ray; 2.30 A; A/B/C/D=1-252.
DR PDB; 5KH4; X-ray; 3.20 A; A/B=1-252.
DR PDB; 5KH5; X-ray; 2.63 A; A/B=1-252.
DR PDBsum; 5KH2; -.
DR PDBsum; 5KH4; -.
DR PDBsum; 5KH5; -.
DR AlphaFoldDB; Q97SR4; -.
DR SMR; Q97SR4; -.
DR IntAct; Q97SR4; 19.
DR STRING; 170187.SP_0261; -.
DR BindingDB; Q97SR4; -.
DR ChEMBL; CHEMBL1075025; -.
DR EnsemblBacteria; AAK74439; AAK74439; SP_0261.
DR GeneID; 60232682; -.
DR GeneID; 66805470; -.
DR KEGG; spn:SP_0261; -.
DR eggNOG; COG0020; Bacteria.
DR OMA; PRTEGHK; -.
DR PhylomeDB; Q97SR4; -.
DR BioCyc; SPNE170187:G1FZB-268-MON; -.
DR BRENDA; 2.5.1.31; 1960.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd00475; Cis_IPPS; 1.
DR Gene3D; 3.40.1180.10; -; 1.
DR HAMAP; MF_01139; ISPT; 1.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR018520; UPP_synth-like_CS.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR10291; PTHR10291; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
DR TIGRFAMs; TIGR00055; uppS; 1.
DR PROSITE; PS01066; UPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..252
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123690"
FT ACT_SITE 28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 28
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 29..32
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 73..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 41..62
FT /evidence="ECO:0007829|PDB:5KH2"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 74..78
FT /evidence="ECO:0007829|PDB:5KH4"
FT HELIX 80..97
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:5KH2"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 120..133
FT /evidence="ECO:0007829|PDB:5KH2"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:5KH2"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5KH2"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5KH2"
FT TURN 212..217
FT /evidence="ECO:0007829|PDB:5KH2"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:5KH2"
FT HELIX 232..245
FT /evidence="ECO:0007829|PDB:5KH2"
SQ SEQUENCE 252 AA; 28705 MW; 4859F158422293D6 CRC64;
MFGFFKKDKA VEVEVPTQVP AHIGIIMDGN GRWAKKRMQP RVFGHKAGME ALQTVTKAAN
KLGVKVITVY AFSTENWTRP DQEVKFIMNL PVEFYDNYVP ELHANNVKIQ MIGETDRLPK
QTFEALTKAE ELTKNNTGLI LNFALNYGGR AEITQALKLI SQDVLDAKIN PGDITEELIG
NYLFTQHLPK DLRDPDLIIR TSGELRLSNF LPWQGAYSEL YFTDTLWPDF DEAALQEAIL
AYNRRHRRFG GV
