ID   EARP_NEIME              Reviewed;         382 AA.
AC   A0A0T7AQA7;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Protein-arginine rhamnosyltransferase {ECO:0000305};
DE            EC=2.4.1.- {ECO:0000305|PubMed:26840407};
DE   AltName: Full=EF-P arginine rhamnosyltransferase {ECO:0000303|PubMed:26840407};
GN   Name=earP {ECO:0000303|PubMed:26840407};
OS   Neisseria meningitidis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=487;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=NIID280 {ECO:0000312|EMBL:BAU19337.1};
RX   PubMed=26840407; DOI=10.1371/journal.pone.0147907;
RA   Yanagisawa T., Takahashi H., Suzuki T., Masuda A., Dohmae N., Yokoyama S.;
RT   "Neisseria meningitidis translation elongation factor P and its active-site
RT   arginine residue are essential for cell viability.";
RL   PLoS ONE 11:e0147907-e0147907(2016).
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:26840407}.
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:0000305|PubMed:26840407};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66693;
CC         Evidence={ECO:0000305|PubMed:26840407};
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   -!- DISRUPTION PHENOTYPE: Leads to much slower cell growth.
CC       {ECO:0000269|PubMed:26840407}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 104 family.
CC       {ECO:0000305}.
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DR   EMBL; LC059993; BAU19337.1; -; Genomic_DNA.
DR   RefSeq; WP_002239014.1; NZ_QSWN01000015.1.
DR   AlphaFoldDB; A0A0T7AQA7; -.
DR   SMR; A0A0T7AQA7; -.
DR   GO; GO:0106361; F:protein-arginine rhamnosyltransferase activity; IDA:UniProtKB.
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; Transferase.
FT   CHAIN           1..382
FT                   /note="Protein-arginine rhamnosyltransferase"
FT                   /id="PRO_0000452679"
FT   ACT_SITE        20
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT   ACT_SITE        270
FT                   /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT   BINDING         17..20
FT                   /ligand="dTDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:57510"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT   BINDING         187
FT                   /ligand="dTDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:57510"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT   BINDING         252
FT                   /ligand="dTDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:57510"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT   BINDING         268..272
FT                   /ligand="dTDP-beta-L-rhamnose"
FT                   /ligand_id="ChEBI:CHEBI:57510"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
SQ   SEQUENCE   382 AA;  43896 MW;  6978EC5E4B44C119 CRC64;
     MNTPPFVCWI FCKVIDNFGD IGVSLRLARV LHRELGWQVH LWTDDVSALR ALCPDLPDVP
     CVHQDIHVRT WHSDAADIDT APVPDAVIET FACDLPENVL HIIRRHKPLW LNWEYLSAEE
     SNERLHLMPS PQEGVQKYFW FMGFSEKSGG LIRERDYRDA VRFDTEALRQ RLMLPEKNAP
     EWLLFGYRSD VWAKWLEMWQ QAGSPMTLLL AGAQIIDSLK QSGIIPQNAL QNDGDVFQTA
     SVRLVKIPFV PQQDFDQLLH LADCAVIRGE DSFVRAQLAG KPFFWHIYPQ DEHVHLDKLH
     AFWDKAHGFY TPETASAHRC LSDDLNGGEA LSATQRLECW QILQQHQNGW RQGAGAWSRY
     LFGQPSASEK LAAFVSKHQK IR