ISPT_STAAN
ID ISPT_STAAN Reviewed; 256 AA.
AC P60477; Q99UL2;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=SA1103;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(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 -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_01139}.
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DR EMBL; BA000018; BAB42355.1; -; Genomic_DNA.
DR PIR; G89899; G89899.
DR RefSeq; WP_000473699.1; NC_002745.2.
DR PDB; 4H8E; X-ray; 1.30 A; A=1-256.
DR PDB; 4U82; X-ray; 1.66 A; A=1-256.
DR PDBsum; 4H8E; -.
DR PDBsum; 4U82; -.
DR AlphaFoldDB; P60477; -.
DR SMR; P60477; -.
DR EnsemblBacteria; BAB42355; BAB42355; BAB42355.
DR KEGG; sau:SA1103; -.
DR HOGENOM; CLU_038505_1_1_9; -.
DR OMA; PRTEGHK; -.
DR Proteomes; UP000000751; 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..256
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123673"
FT ACT_SITE 33
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 33
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 38
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 78..80
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 207..209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT BINDING 220
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01139"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 46..67
FT /evidence="ECO:0007829|PDB:4H8E"
FT STRAND 70..78
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 86..109
FT /evidence="ECO:0007829|PDB:4H8E"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:4H8E"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:4H8E"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 154..171
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 181..185
FT /evidence="ECO:0007829|PDB:4H8E"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:4H8E"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:4H8E"
FT TURN 213..218
FT /evidence="ECO:0007829|PDB:4H8E"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4H8E"
FT HELIX 233..245
FT /evidence="ECO:0007829|PDB:4H8E"
SQ SEQUENCE 256 AA; 29862 MW; 051AE0C3457D0305 CRC64;
MFKKLINKKN TINNYNEELD SSNIPEHIAI IMDGNGRWAK KRKMPRIKGH YEGMQTIKKI
TRIASDIGVK YLTLYAFSTE NWSRPESEVN YIMNLPVNFL KTFLPELIEK NVKVETIGFT
DKLPKSTIEA INNAKEKTAN NTGLKLIFAI NYGGRAELVH SIKNMFDELH QQGLNSDIID
ETYINNHLMT KDYPDPELLI RTSGEQRISN FLIWQVSYSE FIFNQKLWPD FDEDELIKCI
KIYQSRQRRF GGLSEE
