MURE_ARATH
ID MURE_ARATH Reviewed; 772 AA.
AC F4I3P9; Q9CAD3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic {ECO:0000305};
DE Short=AtMurE {ECO:0000303|PubMed:18036201};
DE AltName: Full=Protein ALBINO OR PALE-GREEN 13 {ECO:0000303|PubMed:18036201};
DE AltName: Full=Protein PIGMENT DEFECTIVE EMBRYO 316 {ECO:0000305};
DE Flags: Precursor;
GN Name=MURE {ECO:0000303|PubMed:18036201};
GN Synonyms=APG13 {ECO:0000303|PubMed:18036201}, PDE316 {ECO:0000305};
GN OrderedLocusNames=At1g63680 {ECO:0000312|Araport:AT1G63680};
GN ORFNames=F24D7.13 {ECO:0000312|EMBL:AAG52413.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16326926; DOI=10.1105/tpc.105.036392;
RA Pfalz J., Liere K., Kandlbinder A., Dietz K.-J., Oelmueller R.;
RT "pTAC2, -6, and -12 are components of the transcriptionally active plastid
RT chromosome that are required for plastid gene expression.";
RL Plant Cell 18:176-197(2006).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18036201; DOI=10.1111/j.1365-313x.2007.03379.x;
RA Garcia M., Myouga F., Takechi K., Sato H., Nabeshima K., Nagata N.,
RA Takio S., Shinozaki K., Takano H.;
RT "An Arabidopsis homolog of the bacterial peptidoglycan synthesis enzyme
RT MurE has an essential role in chloroplast development.";
RL Plant J. 53:924-934(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Involved in chloroplast biogenesis. Required for thylakoid
CC membrane development. Seems to be required for plastid-encoded plastid
CC RNA polymerase (PEP)-dependent gene expression.
CC {ECO:0000269|PubMed:18036201}.
CC -!- SUBUNIT: Component of the plastid-encoded plastid RNA polymerase (PEP)
CC complex. {ECO:0000269|PubMed:16326926}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:18036201}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC {ECO:0000269|PubMed:18036201}.
CC -!- DISRUPTION PHENOTYPE: Albino phenotype and seedling lethality under
CC normal growth conditions. {ECO:0000269|PubMed:18036201}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52413.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011622; AAG52413.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34132.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59538.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59539.1; -; Genomic_DNA.
DR PIR; G96661; G96661.
DR RefSeq; NP_001321888.1; NM_001334121.1.
DR RefSeq; NP_001321889.1; NM_001334120.1.
DR RefSeq; NP_176555.4; NM_105045.6.
DR AlphaFoldDB; F4I3P9; -.
DR SMR; F4I3P9; -.
DR STRING; 3702.AT1G63680.1; -.
DR iPTMnet; F4I3P9; -.
DR PaxDb; F4I3P9; -.
DR PRIDE; F4I3P9; -.
DR ProteomicsDB; 251409; -.
DR EnsemblPlants; AT1G63680.1; AT1G63680.1; AT1G63680.
DR EnsemblPlants; AT1G63680.2; AT1G63680.2; AT1G63680.
DR EnsemblPlants; AT1G63680.3; AT1G63680.3; AT1G63680.
DR GeneID; 842672; -.
DR Gramene; AT1G63680.1; AT1G63680.1; AT1G63680.
DR Gramene; AT1G63680.2; AT1G63680.2; AT1G63680.
DR Gramene; AT1G63680.3; AT1G63680.3; AT1G63680.
DR KEGG; ath:AT1G63680; -.
DR Araport; AT1G63680; -.
DR TAIR; locus:2026699; AT1G63680.
DR eggNOG; ENOG502QTHZ; Eukaryota.
DR HOGENOM; CLU_022291_4_0_1; -.
DR InParanoid; F4I3P9; -.
DR OMA; FIPGRML; -.
DR OrthoDB; 1363473at2759; -.
DR PRO; PR:F4I3P9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4I3P9; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0042644; C:chloroplast nucleoid; HDA:TAIR.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 1.
DR HAMAP; MF_00208; MurE; 1.
DR InterPro; IPR036565; Mur-like_cat_sf.
DR InterPro; IPR004101; Mur_ligase_C.
DR InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR InterPro; IPR013221; Mur_ligase_cen.
DR InterPro; IPR000713; Mur_ligase_N.
DR InterPro; IPR035911; MurE/MurF_N.
DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR Pfam; PF01225; Mur_ligase; 1.
DR Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR SUPFAM; SSF63418; SSF63418; 1.
DR TIGRFAMs; TIGR01085; murE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Phosphoprotein; Plastid; Reference proteome; Transcription;
KW Transcription regulation; Transit peptide.
FT TRANSIT 1..40
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 41..772
FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT diaminopimelate ligase MurE homolog, chloroplastic"
FT /id="PRO_0000441845"
FT REGION 42..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 772 AA; 85587 MW; F94C5CB71653887D CRC64;
MAFTFLSPHP VFLSLTGTTS SFSYKPVLLP FSRNSRTLTV AAGPARRNSY PNPADDDPPE
APEDSMHGVS KFQQIQRQAA RARKLEEEDF EKNRNTYLSA IADVEDAAET GRDDEESGGD
LFSDIDRAIS MKRSEFVKQG LLKPNPPKTA SLKKIGEEGN EEEGDVTDDV DELDEEEVVD
LDEIDKLTGL TEISDEEDWV DEEGNTRINK KKEFGSDHQF EFDLDDFGES KARIVEPKFK
MCLAELLDES KVVPISVYGD LDVEITGIQH DSRGVSAGDL FVCCLGSENF LSEADKRGAV
AVVASKEIDI EDTLGCRALV IVEDTNAVLA ALASSFYRHP SKNMSVIGVT GTDGKTTTTY
LIKSLYEAMG VRTGMFSTVS CYIHGDNKLD TPNATMNPDA VLVQSLMAKM LHNGTESLVM
EASPQELALG KCDEVDFDIA VFTNLTRENT DFRGTDEEYR DAEAKLFSRM VDPERHRKVV
NIDDPNAAFF VQQGNPNVPV VTFAMENTKA DVHPLKFELS LFETQVLVNT PQGILEISSG
LLGRHNIYNI LAAVAVGIAV GAPLEDIVRG VEEVDAVPGR CELIDEEQAF GVIVDHANTP
DGLSRLLDSI RELKPRRIIT VIGCEGENER GKRPLMTKIA TEKSDVTMLT SDNPRNEDPL
DILDDMLSGI GWTMQEYLKH GEHDYYPPLA NGHRLFLHDI RRVAVRCAVA MGEEGDMVVV
AGKGHEAYQL EGEKKEFYDD REECREALQY VDELHQAGID TSEFPWRLPE SH
