MRAY_ARATH
ID MRAY_ARATH Reviewed; 480 AA.
AC O49730; Q8L7I8; Q9M0M0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase homolog;
DE AltName: Full=Translocase I;
GN Name=TRANS11; OrderedLocusNames=At4g18270; ORFNames=T9A21.120;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-480, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE (ISOFORM 1).
RC STRAIN=cv. Landsberg erecta;
RA Mondego J.M.C., Simoes-Araujo J.L., Oliveira D.E., Alves-Ferreira M.;
RT "A gene similar to bacterial translocase I (mra Y) identified by cDNA-AFLP
RT is expressed during flower bud development of Arabidopsis thaliana.";
RL Plant Sci. 164:323-331(2003).
CC -!- FUNCTION: May be involved in glycosylation events.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O49730-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O49730-2; Sequence=VSP_036633, VSP_036634;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in flowers and siliques
CC (tapetum and ovule inner integument), but also found in roots, stems
CC and leaves.
CC -!- DEVELOPMENTAL STAGE: Expressed during late flower bud development.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX826626; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAA16799.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78829.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL021713; CAA16799.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161548; CAB78829.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84018.1; -; Genomic_DNA.
DR EMBL; BX826626; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY130289; AAM94346.1; -; mRNA.
DR PIR; F85205; F85205.
DR PIR; T04929; T04929.
DR RefSeq; NP_193561.4; NM_117937.5. [O49730-1]
DR AlphaFoldDB; O49730; -.
DR SMR; O49730; -.
DR STRING; 3702.AT4G18270.1; -.
DR PaxDb; O49730; -.
DR PRIDE; O49730; -.
DR EnsemblPlants; AT4G18270.1; AT4G18270.1; AT4G18270. [O49730-1]
DR GeneID; 827553; -.
DR Gramene; AT4G18270.1; AT4G18270.1; AT4G18270. [O49730-1]
DR KEGG; ath:AT4G18270; -.
DR Araport; AT4G18270; -.
DR TAIR; locus:2141892; AT4G18270.
DR eggNOG; ENOG502QPYQ; Eukaryota.
DR HOGENOM; CLU_023982_0_2_1; -.
DR InParanoid; O49730; -.
DR OMA; ICSELAI; -.
DR OrthoDB; 1301087at2759; -.
DR PhylomeDB; O49730; -.
DR BioCyc; ARA:AT4G18270-MON; -.
DR PRO; PR:O49730; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O49730; baseline and differential.
DR Genevisible; O49730; AT.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IBA:GO_Central.
DR GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR CDD; cd06852; GT_MraY; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR PANTHER; PTHR22926; PTHR22926; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
DR TIGRFAMs; TIGR00445; mraY; 1.
DR PROSITE; PS01347; MRAY_1; 1.
DR PROSITE; PS01348; MRAY_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..480
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase
FT homolog"
FT /id="PRO_0000108938"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 287..290
FT /note="KMLV -> YSLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036633"
FT VAR_SEQ 291..480
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_036634"
FT CONFLICT 187
FT /note="L -> F (in Ref. 1; AAM94346)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="N -> T (in Ref. 1; AAM94346)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="T -> P (in Ref. 1; AAM94346)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="I -> V (in Ref. 1; AAM94346)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 51720 MW; 78DF36F3E685EE66 CRC64;
MRCSLLTPTS YRFHYPNPFR SLESIPPLSN SRYRIESGSP SSFKFSAPSL QRHSSVSVKA
FDDDTFDFYT GDIFAATYAI SSSEGEESDG DYALNVVTET TAQKLGKFPR GRKKHRIRYG
INLGLLAFLS LLLLLMDSFA WKIVRLPLPP YFLSMPFFTS AILVTLAGYI FVPLLDRLRV
HEPIRTLGPV PHNRRPTIPT MGGLFFVPIG VVVAIALNKV SSIEVLGAAA ATVAFAAIGL
IDDSLSLYSE NNNGLSAKIQ LLLEAAVGTC FAFWLETASL SSPYGMKMLV PLPSPLGLVF
LGKLYLLLTS FYFVSMGNLV KATDGLDGLA GGIAALCFVA MAIAVLPICS DLSVFGASMA
GACFGFLLHN RYRASVSMGD TGSLALGGAL AAMAACSGMF FPLFISSGVA VLEASSVIIQ
VVYYSTTKRL KGKGRRIFKT IPFHHHLRLN GLKEPMIVTM AYVISSLLSL SAAYIGLISA
