ISPT_CAMJE
ID ISPT_CAMJE Reviewed; 222 AA.
AC Q9PP99; Q0PA66;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Isoprenyl transferase;
DE EC=2.5.1.-;
GN Name=uppS; OrderedLocusNames=Cj0824;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND
RP SUBUNIT.
RA Nocek B., Gu M., Grimshaw S., Anderson W.F., Joachimiak A.;
RT "Crystal structure of a probable undecaprenyl diphosph synthase (upps) from
RT campylobacter jejuni.";
RL Submitted (NOV-2011) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the condensation of isopentenyl diphosphate (IPP)
CC with allylic pyrophosphates generating different type of terpenoids.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
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DR EMBL; AL111168; CAL34952.1; -; Genomic_DNA.
DR PIR; H81354; H81354.
DR RefSeq; WP_002852565.1; NC_002163.1.
DR RefSeq; YP_002344231.1; NC_002163.1.
DR PDB; 3UGS; X-ray; 2.46 A; A/B=1-222.
DR PDBsum; 3UGS; -.
DR AlphaFoldDB; Q9PP99; -.
DR SMR; Q9PP99; -.
DR IntAct; Q9PP99; 11.
DR STRING; 192222.Cj0824; -.
DR PaxDb; Q9PP99; -.
DR PRIDE; Q9PP99; -.
DR EnsemblBacteria; CAL34952; CAL34952; Cj0824.
DR GeneID; 905127; -.
DR KEGG; cje:Cj0824; -.
DR PATRIC; fig|192222.6.peg.812; -.
DR eggNOG; COG0020; Bacteria.
DR HOGENOM; CLU_038505_1_1_7; -.
DR OMA; PRTEGHK; -.
DR Proteomes; UP000000799; 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; Reference proteome; Transferase.
FT CHAIN 1..222
FT /note="Isoprenyl transferase"
FT /id="PRO_0000123587"
FT ACT_SITE 12
FT /evidence="ECO:0000250"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 13..16
FT /ligand="substrate"
FT BINDING 17
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57..59
FT /ligand="substrate"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:3UGS"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 65..85
FT /evidence="ECO:0007829|PDB:3UGS"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:3UGS"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:3UGS"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:3UGS"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3UGS"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:3UGS"
FT TURN 183..188
FT /evidence="ECO:0007829|PDB:3UGS"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:3UGS"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:3UGS"
SQ SEQUENCE 222 AA; 26087 MW; D8F42F7967EA8712 CRC64;
MNELKHLAVV MDGNRRWARA KGFLAKLGYS QGVKTMQKLM EVCMEENISN LSLFAFSTEN
WKRPKDEIDF IFELLDRCLD EALEKFEKNN VRLRAIGDLS RLEDKVREKI TLVEEKTKHC
DALCVNLAIS YGARDEIIRA AKRVIEKKLE LNEENLTQNL DLPLDVDLML RVGNAKRLSN
FLLWQCSYAE IYFSETLFPS LTKREFKRII KEFRNRERTF GK
