ID   PGTB2_YEAST             Reviewed;         325 AA.
AC   P20133; D6W4H7; P32433;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 3.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Geranylgeranyl transferase type-2 subunit beta;
DE            EC=2.5.1.60;
DE   AltName: Full=Geranylgeranyl transferase type II subunit beta;
DE            Short=GGTase-II-beta;
DE   AltName: Full=Type II protein geranyl-geranyltransferase subunit beta;
DE            Short=PGGT;
DE   AltName: Full=YPT1/SEC4 proteins geranylgeranyltransferase subunit beta;
GN   Name=BET2; OrderedLocusNames=YPR176C; ORFNames=P9705.12;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2204247; DOI=10.1002/yea.320060407;
RA   Petersen-Bjoern S., Harrington T.R., Friesen J.D.;
RT   "An essential gene in Saccharomyces cerevisiae shares an upstream
RT   regulatory element with PRP4.";
RL   Yeast 6:345-352(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1903184; DOI=10.1038/351158a0;
RA   Rossi G., Jiang Y., Newman A.P., Ferro-Novick S.;
RT   "Dependence of Ypt1 and Sec4 membrane attachment on Bet2.";
RL   Nature 351:158-161(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187.
RX   PubMed=2528686; DOI=10.1128/mcb.9.9.3698-3709.1989;
RA   Petersen-Bjoern S., Soltyk A., Beggs J.D., Friesen J.D.;
RT   "PRP4 (RNA4) from Saccharomyces cerevisiae: its gene product is associated
RT   with the U4/U6 small nuclear ribonucleoprotein particle.";
RL   Mol. Cell. Biol. 9:3698-3709(1989).
RN   [7]
RP   CHARACTERIZATION.
RX   PubMed=8232542; DOI=10.1038/366084a0;
RA   Jiang Y., Rossi G., Ferro-Novick S.;
RT   "Bet2p and Mad2p are components of a prenyltransferase that adds
RT   geranylgeranyl onto Ypt1p and Sec4p.";
RL   Nature 366:84-86(1993).
RN   [8]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Catalyzes the transfer of a geranyl-geranyl moiety from
CC       geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or
CC       -XCXC, where both cysteines may become modified. Acts on YPT1 and SEC4.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=geranylgeranyl diphosphate + L-cysteinyl-[protein] =
CC         diphosphate + S-geranylgeranyl-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:21240, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11537,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:57533,
CC         ChEBI:CHEBI:86021; EC=2.5.1.60;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- INTERACTION:
CC       P20133; Q00618: BET4; NbExp=3; IntAct=EBI-3559, EBI-3573;
CC   -!- MISCELLANEOUS: Present with 1520 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family. {ECO:0000305}.
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DR   EMBL; M29585; AAA66939.1; -; Genomic_DNA.
DR   EMBL; M26597; AAA79331.1; -; Genomic_DNA.
DR   EMBL; U25842; AAB68110.1; -; Genomic_DNA.
DR   EMBL; AY558067; AAS56393.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11593.1; -; Genomic_DNA.
DR   PIR; S59834; S59834.
DR   RefSeq; NP_015502.1; NM_001184273.1.
DR   AlphaFoldDB; P20133; -.
DR   SMR; P20133; -.
DR   BioGRID; 36349; 358.
DR   ComplexPortal; CPX-1636; Protein geranylgeranyltransferase type II complex.
DR   DIP; DIP-2214N; -.
DR   IntAct; P20133; 3.
DR   STRING; 4932.YPR176C; -.
DR   MaxQB; P20133; -.
DR   PaxDb; 4932-YPR176C; -.
DR   PeptideAtlas; P20133; -.
DR   EnsemblFungi; YPR176C_mRNA; YPR176C; YPR176C.
DR   GeneID; 856306; -.
DR   KEGG; sce:YPR176C; -.
DR   AGR; SGD:S000006380; -.
DR   SGD; S000006380; BET2.
DR   VEuPathDB; FungiDB:YPR176C; -.
DR   eggNOG; KOG0366; Eukaryota.
DR   GeneTree; ENSGT00950000183128; -.
DR   HOGENOM; CLU_028946_3_0_1; -.
DR   InParanoid; P20133; -.
DR   OMA; VKRCQCP; -.
DR   OrthoDB; 5478505at2759; -.
DR   BioCyc; YEAST:MONOMER3O-1; -.
DR   Reactome; R-SCE-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
DR   Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR   BioGRID-ORCS; 856306; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P20133; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; P20133; Protein.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IDA:SGD.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IDA:SGD.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:SGD.
DR   GO; GO:0018344; P:protein geranylgeranylation; IDA:SGD.
DR   GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR   CDD; cd02894; GGTase-II; 1.
DR   Gene3D; 1.50.10.20; -; 1.
DR   InterPro; IPR001330; PFTB_repeat.
DR   InterPro; IPR045089; PGGT1B-like.
DR   InterPro; IPR026873; Ptb1.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1.
DR   PANTHER; PTHR11774:SF11; GERANYLGERANYL TRANSFERASE TYPE-2 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..325
FT                   /note="Geranylgeranyl transferase type-2 subunit beta"
FT                   /id="PRO_0000119777"
FT   REPEAT          9..50
FT                   /note="PFTB 1"
FT   REPEAT          57..99
FT                   /note="PFTB 2"
FT   REPEAT          109..150
FT                   /note="PFTB 3"
FT   REPEAT          157..198
FT                   /note="PFTB 4"
FT   REPEAT          208..249
FT                   /note="PFTB 5"
FT   REPEAT          256..298
FT                   /note="PFTB 6"
FT   BINDING         183..185
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..240
FT                   /ligand="geranylgeranyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57533"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         286
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        22
FT                   /note="K -> N (in Ref. 1 and 5)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   325 AA;  36666 MW;  6A9C44DFBE62AAFC CRC64;
     MSGSLTLLKE KHIRYIESLD TKKHNFEYWL TEHLRLNGIY WGLTALCVLD SPETFVKEEV
     ISFVLSCWDD KYGAFAPFPR HDAHLLTTLS AVQILATYDA LDVLGKDRKV RLISFIRGNQ
     LEDGSFQGDR FGEVDTRFVY TALSALSILG ELTSEVVDPA VDFVLKCYNF DGGFGLCPNA
     ESHAAQAFTC LGALAIANKL DMLSDDQLEE IGWWLCERQL PEGGLNGRPS KLPDVCYSWW
     VLSSLAIIGR LDWINYEKLT EFILKCQDEK KGGISDRPEN EVDVFHTVFG VAGLSLMGYD
     NLVPIDPIYC MPKSVTSKFK KYPYK
//