ID   FNTB_PEA                Reviewed;         419 AA.
AC   Q04903;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein farnesyltransferase subunit beta;
DE            Short=FTase-beta;
DE            EC=2.5.1.58;
DE   AltName: Full=CAAX farnesyltransferase subunit beta;
DE   AltName: Full=Ras proteins prenyltransferase subunit beta;
GN   Name=FTB;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND
RP   COFACTOR.
RC   STRAIN=cv. Alaska; TISSUE=Seedling;
RX   PubMed=8278509; DOI=10.1104/pp.101.2.667;
RA   Yang Z., Cramer C.L., Watson J.C.;
RT   "Protein farnesyltransferase in plants. Molecular cloning and expression of
RT   a homolog of the beta subunit from the garden pea.";
RL   Plant Physiol. 101:667-674(1993).
CC   -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl
CC       diphosphate to a cysteine at the fourth position from the C-terminus of
CC       several proteins. The beta subunit FTB is responsible for peptide-
CC       binding. {ECO:0000269|PubMed:8278509}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019,
CC         ChEBI:CHEBI:175763; EC=2.5.1.58;
CC         Evidence={ECO:0000269|PubMed:8278509};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:8278509};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:8278509};
CC   -!- SUBUNIT: Heterodimer of FTA and FTB. {ECO:0000269|PubMed:8278509}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; L08664; AAA33649.1; -; mRNA.
DR   PIR; JQ2254; JQ2254.
DR   AlphaFoldDB; Q04903; -.
DR   SMR; Q04903; -.
DR   PRIDE; Q04903; -.
DR   GO; GO:0005965; C:protein farnesyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0018343; P:protein farnesylation; ISS:UniProtKB.
DR   CDD; cd02893; FTase; 1.
DR   InterPro; IPR026872; FTB.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; PTHR11774; 1.
DR   PANTHER; PTHR11774:SF6; PTHR11774:SF6; 1.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SUPFAM; SSF48239; SSF48239; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Prenyltransferase; Repeat; Transferase; Zinc.
FT   CHAIN           1..419
FT                   /note="Protein farnesyltransferase subunit beta"
FT                   /id="PRO_0000119765"
FT   REPEAT          68..109
FT                   /note="PFTB 1"
FT   REPEAT          119..160
FT                   /note="PFTB 2"
FT   REPEAT          167..208
FT                   /note="PFTB 3"
FT   REPEAT          215..256
FT                   /note="PFTB 4"
FT   REPEAT          329..371
FT                   /note="PFTB 5"
FT   BINDING         193..196
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         235..238
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         241
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         243
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         244..247
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         359
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   SITE            47
FT                   /note="Important for selectivity against geranylgeranyl
FT                   diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
SQ   SEQUENCE   419 AA;  46794 MW;  4F040E0094277D7C CRC64;
     MEASTAAETP TPTVSQRDQW IVESQVFHIY QLFANIPPNA QSIIRPWLCY WIIHSIALLG
     ESIDDDLEDN TVDFLNRCQD PNGGYAGGPG QMPHLATTYA AVNTLITLGG EKSLASINRN
     KLYGFMRRMK QPNGGFRMHD EGEIDVRACY TAISVASVLN ILDDELIKNV GDFILSCQTY
     EGGLAGEPGS EAHGGYTFCG LAAMILIGEV NRLDLPRLLD WVVFRQGKEC GFQGRTNKLV
     DGCYSFWQGG AVALLQRLHS IIDEQMAEAS QFVTVSDAPE EKECLDGTSS HATSHIRHEG
     MNESCSSDVK NIGYNFISEW RQSEPLFHSI ALQQYILLCS QEQDGGLRDK PGKRRDHYHS
     CYCLSGLSLC QYSWSKRPDS PPLPKVVMGP YSNLLEPIHP LFNVVLDRYR EAHEFFSQL