ID   FNTB_SCHPO              Reviewed;         382 AA.
AC   O13782;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Protein farnesyltransferase subunit beta;
DE            Short=FTase-beta;
DE            EC=2.5.1.58 {ECO:0000269|PubMed:10617635};
DE   AltName: Full=CAAX farnesyltransferase subunit beta;
DE   AltName: Full=Ras proteins prenyltransferase subunit beta;
GN   Name=cpp1; ORFNames=SPAC17G6.04c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RX   PubMed=10617635; DOI=10.1074/jbc.275.1.429;
RA   Yang W., Urano J., Tamanoi F.;
RT   "Protein farnesylation is critical for maintaining normal cell morphology
RT   and canavanine resistance in Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 275:429-438(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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(cpp1) subunit is responsible for peptide-
CC       binding. {ECO:0000269|PubMed:10617635}.
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:10617635};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13346;
CC         Evidence={ECO:0000269|PubMed:10617635};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P49356};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P49356};
CC   -!- SUBUNIT: Heterodimer of an alpha(cwp1) and a beta(cpp1) subunit.
CC       {ECO:0000269|PubMed:10617635}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB16215.1; -; Genomic_DNA.
DR   PIR; T37836; T37836.
DR   RefSeq; NP_594251.1; NM_001019674.2.
DR   AlphaFoldDB; O13782; -.
DR   SMR; O13782; -.
DR   BioGRID; 278844; 13.
DR   STRING; 284812.O13782; -.
DR   MaxQB; O13782; -.
DR   PaxDb; 4896-SPAC17G6-04c-1; -.
DR   EnsemblFungi; SPAC17G6.04c.1; SPAC17G6.04c.1:pep; SPAC17G6.04c.
DR   GeneID; 2542380; -.
DR   KEGG; spo:SPAC17G6.04c; -.
DR   PomBase; SPAC17G6.04c; cpp1.
DR   VEuPathDB; FungiDB:SPAC17G6.04c; -.
DR   eggNOG; KOG0365; Eukaryota.
DR   HOGENOM; CLU_028946_0_2_1; -.
DR   InParanoid; O13782; -.
DR   OMA; WCIYWIL; -.
DR   PhylomeDB; O13782; -.
DR   Reactome; R-SPO-9648002; RAS processing.
DR   PRO; PR:O13782; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0005965; C:protein farnesyltransferase complex; IPI:PomBase.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; IDA:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IC:PomBase.
DR   CDD; cd02893; FTase; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR026872; FTB.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1.
DR   PANTHER; PTHR11774:SF6; PROTEIN FARNESYLTRANSFERASE SUBUNIT BETA; 1.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Prenyltransferase; Reference proteome; Repeat; Transferase;
KW   Zinc.
FT   CHAIN           1..382
FT                   /note="Protein farnesyltransferase subunit beta"
FT                   /id="PRO_0000119767"
FT   REPEAT          78..119
FT                   /note="PFTB 1"
FT   REPEAT          129..170
FT                   /note="PFTB 2"
FT   REPEAT          178..219
FT                   /note="PFTB 3"
FT   REPEAT          226..268
FT                   /note="PFTB 4"
FT   REPEAT          286..328
FT                   /note="PFTB 5"
FT   BINDING         204..207
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         247..250
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         256..259
FT                   /ligand="(2E,6E)-farnesyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:175763"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
FT   SITE            58
FT                   /note="Important for selectivity against geranylgeranyl
FT                   diphosphate"
FT                   /evidence="ECO:0000250|UniProtKB:P49356"
SQ   SEQUENCE   382 AA;  42189 MW;  C3F2705D93F84203 CRC64;
     MDELSETQVM QNETATAVLP LLNGESQSFN LQKHLKYLTK MLDPLPSPFT VLDASRAWMV
     YWELSSLAIL GKLDSSVCER AISSVRQLKG PSGGFCGGNG QDEHLLSTYA SILSICLCDS
     TDAYSLIERD RLYDWLFSLK NPDGSFRVNN EGESDARSVY AAVCVSSLVG ISMDDPLFEG
     TLQWLCKCQT YEGGLSGVPY AEAHGGYTFC ALAAIALLGG LDNLNEIKLS TWLVQRQDPA
     LYGFSGRSNK LVDGCYSWWV GASHVIVASG YGSASHKSLP NLFYNPEKLL GYILQCCQST
     SGGLRDKPPK RPDQYHTCYC LLGLSSIAYD YRYHTSDGWS YKPSILHSSL SSLLPAHPIY
     CVPFGFEERI KSYFLSQESS KF
//