EARP_SHEON
ID EARP_SHEON Reviewed; 395 AA.
AC Q8EEP8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Protein-arginine rhamnosyltransferase {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:25686373};
DE AltName: Full=EF-P arginine rhamnosyltransferase {ECO:0000303|PubMed:25686373};
GN Name=earP {ECO:0000303|PubMed:25686373};
GN OrderedLocusNames=SO_2329 {ECO:0000312|EMBL:AAN55363.1};
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25686373; DOI=10.1038/nchembio.1751;
RA Lassak J., Keilhauer E.C., Fuerst M., Wuichet K., Goedeke J.,
RA Starosta A.L., Chen J.M., Soegaard-Andersen L., Rohr J., Wilson D.N.,
RA Haeussler S., Mann M., Jung K.;
RT "Arginine-rhamnosylation as new strategy to activate translation elongation
RT factor P.";
RL Nat. Chem. Biol. 11:266-270(2015).
CC -!- FUNCTION: Protein-arginine rhamnosyltransferase that catalyzes the
CC transfer of a single rhamnose to elongation factor P (EF-P) on 'Lys-
CC 32', a modification required for EF-P-dependent rescue of polyproline
CC stalled ribosomes. {ECO:0000269|PubMed:25686373}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTDP-beta-L-rhamnose + L-arginyl-[protein] = dTDP + H(+) +
CC N(omega)-(alpha-L-rhamnosyl)-L-arginyl-[protein];
CC Xref=Rhea:RHEA:66692, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:17096,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57510,
CC ChEBI:CHEBI:58369, ChEBI:CHEBI:167445;
CC Evidence={ECO:0000269|PubMed:25686373};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66693;
CC Evidence={ECO:0000269|PubMed:25686373};
CC -!- DOMAIN: Adopts a GT-B fold and acts as an inverting enzyme that
CC converts the beta-configuration in the dTDP-beta-L-rhamnose donor to
CC the alpha configuration in the N-linked (Rha) arginine product.
CC {ECO:0000250|UniProtKB:Q9HZZ1}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 104 family.
CC {ECO:0000305}.
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DR EMBL; AE014299; AAN55363.1; -; Genomic_DNA.
DR RefSeq; NP_717919.1; NC_004347.2.
DR RefSeq; WP_011072321.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EEP8; -.
DR SMR; Q8EEP8; -.
DR STRING; 211586.SO_2329; -.
DR PaxDb; Q8EEP8; -.
DR KEGG; son:SO_2329; -.
DR PATRIC; fig|211586.12.peg.2244; -.
DR eggNOG; COG4394; Bacteria.
DR HOGENOM; CLU_060250_0_0_6; -.
DR OMA; YFFFPGF; -.
DR OrthoDB; 1485314at2; -.
DR PhylomeDB; Q8EEP8; -.
DR BioCyc; SONE211586:G1GMP-2128-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0106361; F:protein-arginine rhamnosyltransferase activity; IEA:InterPro.
DR InterPro; IPR016633; EarP.
DR Pfam; PF10093; EarP; 1.
DR PIRSF; PIRSF015557; UCP015557; 1.
DR TIGRFAMs; TIGR03837; efp_adjacent_2; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..395
FT /note="Protein-arginine rhamnosyltransferase"
FT /id="PRO_0000452683"
FT ACT_SITE 22
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT ACT_SITE 290
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT BINDING 19..22
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT BINDING 205
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT BINDING 272
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT BINDING 288..292
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
SQ SEQUENCE 395 AA; 44758 MW; 077DBC643FEB6A7F CRC64;
MSTSSNASHW DIFCTVVDNY GDIGVTWRLA KQLVNEYHIP IILWVDDLNS FSHILPTLNP
KLVSQCFNGV IINHWTTPLA VPYLPGKVLI EAFACELPDE VKLQLATLHK TAPQAVPLWL
NLEYLSAEDW VDGCHGLPSM QVSGIKKYFY FPGFTPKTGG LICERELFAE RDAWQQDPAN
KLQLFESLGL KDIQAQDSVF SIFSYETDSL PALCELWQAR AKNDAKIHAL LPKGRSLNSL
QHLLPCPVDA LMPGQQIKLG DLTLHILPMT DQQGFDRLLW SCDVNIVRGE DSFLRAQWAA
KPFIWHIYPQ EDDYHLIKLE AFIRLYCDNL APDIADTWSK LNFAFSQGQQ SAVKTHWQNL
NPVSLPLLQH AKEWPIDAIN AADLATRLVQ FVKKS
