PETS_CHLRE
ID PETS_CHLRE Reviewed; 1013 AA.
AC A8J637; Q5QEB2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Polyprotein of EF-Ts, chloroplastic {ECO:0000303|PubMed:15548736};
DE Short=110 kDa pro-protein {ECO:0000303|PubMed:15548736};
DE Contains:
DE RecName: Full=Plastid-specific ribosomal protein-7, chloroplastic {ECO:0000303|PubMed:15548736};
DE Short=65 kDa protein PSRP-7 {ECO:0000303|PubMed:15548736};
DE Short=CrePSRP-7 {ECO:0000303|PubMed:12417713};
DE Contains:
DE RecName: Full=Elongation factor Ts, chloroplastic {ECO:0000303|PubMed:15548736};
DE Short=55 kDa protein EF-Ts {ECO:0000303|PubMed:15548736};
DE Short=EF-Ts {ECO:0000303|PubMed:15548736};
DE Flags: Precursor;
GN Name=PETs {ECO:0000303|PubMed:15548736};
GN Synonyms=EFTS {ECO:0000303|PubMed:15548736},
GN PSRP-7 {ECO:0000303|PubMed:15548736};
GN ORFNames=CHLRE_12g519180v5 {ECO:0000312|EMBL:PNW75255.1},
GN CHLREDRAFT_195617 {ECO:0000312|EMBL:EDP00635.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, PROTEIN
RP SEQUENCE OF 44-48, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, SUBUNIT,
RP TISSUE SPECIFICITY, INDUCTION BY LIGHT, AND GENE FAMILY.
RC STRAIN=137c / CC-125;
RX PubMed=15548736; DOI=10.1105/tpc.104.026708;
RA Beligni M.V., Yamaguchi K., Mayfield S.P.;
RT "Chloroplast elongation factor ts pro-protein is an evolutionarily
RT conserved fusion with the s1 domain-containing plastid-specific ribosomal
RT protein-7.";
RL Plant Cell 16:3357-3369(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=Arg7/cw15;
RX PubMed=12417713; DOI=10.1105/tpc.004341;
RA Yamaguchi K., Prieto S., Beligni M.V., Haynes P.A., McDonald W.H.,
RA Yates J.R. III, Mayfield S.P.;
RT "Proteomic characterization of the small subunit of Chlamydomonas
RT reinhardtii chloroplast ribosome: identification of a novel S1 domain-
RT containing protein and unusually large orthologs of bacterial S2, S3, and
RT S5.";
RL Plant Cell 14:2957-2974(2002).
RN [4]
RP REVIEW ON CHLOROPLAST RIBOSOME SUBUNITS.
RX PubMed=12826678; DOI=10.1074/jbc.m301934200;
RA Yamaguchi K., Beligni M.V., Prieto S., Haynes P.A., McDonald W.H.,
RA Yates J.R. III, Mayfield S.P.;
RT "Proteomic characterization of the Chlamydomonas reinhardtii chloroplast
RT ribosome. Identification of proteins unique to the 70S ribosome.";
RL J. Biol. Chem. 278:33774-33785(2003).
CC -!- FUNCTION: [Elongation factor Ts, chloroplastic]: Associates with the
CC EF-Tu.GDP complex and induces the exchange of GDP to GTP
CC (PubMed:15548736). It remains bound to the aminoacyl-tRNA.EF-Tu.GTP
CC complex up to the GTP hydrolysis stage on the ribosome
CC (PubMed:15548736). {ECO:0000269|PubMed:15548736}.
CC -!- FUNCTION: [Plastid-specific ribosomal protein-7, chloroplastic]: Binds
CC to psbD and psbA mRNAs 5'-untranslated regions (UTRs) in vitro.
CC {ECO:0000269|PubMed:15548736}.
CC -!- SUBUNIT: [Plastid-specific ribosomal protein-7, chloroplastic]:
CC Component of the chloroplast ribosome 30S and 70S subunits, as well as
CC polysomes. {ECO:0000269|PubMed:12417713, ECO:0000269|PubMed:15548736}.
CC -!- SUBUNIT: [Polyprotein of EF-Ts, chloroplastic]: Component of the
CC chloroplast ribosome 70S subunit, and at low levels, present in
CC polysomes. {ECO:0000269|PubMed:15548736}.
CC -!- SUBUNIT: [Elongation factor Ts, chloroplastic]: Associates transiently
CC with chloroplast polysomes. {ECO:0000269|PubMed:15548736}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:12417713, ECO:0000269|PubMed:15548736}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=110 kDa pro-protein {ECO:0000303|PubMed:15548736};
CC IsoId=A8J637-1; Sequence=Displayed;
CC Name=2; Synonyms=79 kDa protein PSRP-7 {ECO:0000303|PubMed:15548736};
CC IsoId=A8J637-2; Sequence=VSP_060529, VSP_060530;
CC Name=3; Synonyms=61 kDa protein PSRP-7 {ECO:0000303|PubMed:15548736};
CC IsoId=A8J637-3; Sequence=VSP_060527, VSP_060528;
CC -!- INDUCTION: [Polyprotein of EF-Ts, chloroplastic]: Visible only at the
CC end of the dark period, in 12 hours light/ 12 hours dark conditions (at
CC protein level) (PubMed:15548736). Induced transiently upon shifting to
CC light; mostly expressed after shifting to light, to a lower extent at
CC the end of the dark period and under continuous light, and at low
CC levels at the end of the light period (PubMed:15548736).
CC {ECO:0000269|PubMed:15548736}.
CC -!- INDUCTION: [Isoform 2]: Induced transiently upon shifting to light;
CC mostly expressed after shifting to light, tand at low levels at the end
CC of the light and dark periods and under continuous light.
CC {ECO:0000269|PubMed:15548736}.
CC -!- INDUCTION: [Isoform 3]: Induced transiently upon shifting to light;
CC mostly expressed after shifting to light, to a lower extent at the end
CC of the dark period and under continuous light, and at low levels at the
CC end of the light period. {ECO:0000269|PubMed:15548736}.
CC -!- INDUCTION: [Plastid-specific ribosomal protein-7, chloroplastic]:
CC Expressed constitutively in both continuous light, and 12 hours light/
CC 12 hours dark conditions (at protein level).
CC {ECO:0000269|PubMed:15548736}.
CC -!- INDUCTION: [Elongation factor Ts, chloroplastic]: Expressed
CC constitutively in both continuous light, and 12 hours light/ 12 hours
CC dark conditions (at protein level). {ECO:0000269|PubMed:15548736}.
CC -!- MISCELLANEOUS: [Plastid-specific ribosomal protein-7, chloroplastic]:
CC 65 kDa protein PSRP-7 is the major form. {ECO:0000269|PubMed:15548736}.
CC -!- SIMILARITY: [Elongation factor Ts, chloroplastic]: Belongs to the EF-Ts
CC family. {ECO:0000305}.
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DR EMBL; AY661459; AAU93598.1; -; mRNA.
DR EMBL; CM008973; PNW75255.1; -; Genomic_DNA.
DR EMBL; DS496138; EDP00635.1; -; Genomic_DNA.
DR RefSeq; XP_001696943.1; XM_001696891.1. [A8J637-1]
DR AlphaFoldDB; A8J637; -.
DR SMR; A8J637; -.
DR STRING; 3055.EDP00635; -.
DR PaxDb; A8J637; -.
DR PRIDE; A8J637; -.
DR ProMEX; A8J637; -.
DR EnsemblPlants; PNW75255; PNW75255; CHLRE_12g519180v5. [A8J637-1]
DR GeneID; 5722614; -.
DR Gramene; PNW75255; PNW75255; CHLRE_12g519180v5. [A8J637-1]
DR KEGG; cre:CHLRE_12g519180v5; -.
DR eggNOG; KOG1071; Eukaryota.
DR HOGENOM; CLU_012395_0_0_1; -.
DR InParanoid; A8J637; -.
DR OrthoDB; 1048278at2759; -.
DR Proteomes; UP000006906; Chromosome 12.
DR ExpressionAtlas; A8J637; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0043253; C:chloroplast ribosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-UniRule.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:1905538; F:polysome binding; IDA:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0061770; F:translation elongation factor binding; IDA:UniProtKB.
DR GO; GO:0009416; P:response to light stimulus; IEP:UniProtKB.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 2.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR018101; Transl_elong_Ts_CS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 2.
DR Pfam; PF00889; EF_TS; 2.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 2.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54713; SSF54713; 2.
DR TIGRFAMs; TIGR00116; tsf; 2.
DR PROSITE; PS01126; EF_TS_1; 2.
DR PROSITE; PS01127; EF_TS_2; 2.
DR PROSITE; PS50126; S1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing;
KW Elongation factor; Plastid; Protein biosynthesis; Reference proteome;
KW Repeat; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:15548736"
FT CHAIN 44..1013
FT /note="Polyprotein of EF-Ts, chloroplastic"
FT /id="PRO_0000449219"
FT CHAIN 44..559
FT /note="Plastid-specific ribosomal protein-7, chloroplastic"
FT /id="PRO_0000449220"
FT CHAIN 560..1013
FT /note="Elongation factor Ts, chloroplastic"
FT /id="PRO_0000449221"
FT DOMAIN 64..133
FT /note="S1 motif 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT DOMAIN 227..331
FT /note="S1 motif 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 141..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..163
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 559..560
FT /note="NI -> SQ (in isoform 3)"
FT /evidence="ECO:0000305|PubMed:15548736"
FT /id="VSP_060527"
FT VAR_SEQ 561..1013
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305|PubMed:15548736"
FT /id="VSP_060528"
FT VAR_SEQ 596..603
FT /note="WLRKKGLS -> VGKRAGFF (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:15548736"
FT /id="VSP_060529"
FT VAR_SEQ 604..1013
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305|PubMed:15548736"
FT /id="VSP_060530"
FT CONFLICT 334
FT /note="E -> K (in Ref. 1; AAU93598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1013 AA; 108770 MW; 5478E2AA7FDE601C CRC64;
MLRELGRTAT VKAHGRSVLR PVRGPAGRRQ VAFTGVRPSV RVFAEAPAAE QAAKAIKLED
VKEGSEYEGT VTTVEEFGAF VNFGANTNGL VHISKLASGF TKNAKDVVQP GQKVTVKVLS
VDAEKKRVSL ELKSAVAAEA SAEESDDIIT EPDREGADAT DDDEDVEVEL EDGQVEVRAD
LPGFEDIPFV MEEADMDAEM SEAAIAALEA DLDGAEIRYE LEAPAYMEEV TGKVARIEDY
GVFLEFEWNG KTLTGLLAKD EMKVPSSALS AEAQAALRAE WADTGFEMPA FVELPDDELD
VKKYYQPGES VPAFVLESSL VDGRGISLTH FTDEEVSAEA VAAYEELEDD EDEELDKMMA
DAAGLEDEVL AFDPEALMEE DEGEEAGAAA DAGDDAEYEG VSADGLEGAN GNYALGATRS
GLIKGKNGYQ VAPMGLPSRP LNDAVTSSGL AILGTSEVDF DGDEVQLVDY WTSEAFDNIP
KDVLKKLGLK MSYTEAGEAE FEERADFEAT DVPFYLYGGD VESRAKEFVA DLLSDDVDEA
ELPARAGRAP IVLAAAVQNI SAAEVKALRE KTGAGMMDCK KALAECAGDA EAAAEWLRKK
GLSGADKKAG RIAAEGAVAR YIHPGSRLGV LLEVNCETDF VAASEKFQAL VNELGMIIAA
TDCICVSPED VPEEVLAKER EVEMGKEDLA NKPEAIRAKI VEGRLQKMRD QVALTNQATL
SNPDKTVAEL VKETIAAVGE NVKIRRFIKY RLGEGLEKKA NDFAAEVAQQ TQAKAAAPAA
PKKEEPKKEE PKKATVAVSA GTVKELRDKT GAGMMDCKKA LAENENDMEK ATEWLRMKGL
AGADKKAGRI AAEGVVASYI HPGSRLGVLL EVNCETDFVA ASEKFNELVN YIAMGIVAGQ
NVQYVSADEI PAEVFEREKQ LEMARDDLKG KPDAIRAKIA EGRAKKIATE MCLLDQPFLT
DPSKTVAEAI KESIAAIGEK ISVRRFVKFQ LGEGLEKKSN DFAAEVAAAT GAK
