EARP_NEIMH
ID EARP_NEIMH Reviewed; 382 AA.
AC E6MVV9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Protein-arginine rhamnosyltransferase {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:29440735};
DE AltName: Full=EF-P arginine rhamnosyltransferase {ECO:0000303|PubMed:29440735};
GN Name=earP {ECO:0000303|PubMed:29440735};
GN ORFNames=NMH_0797 {ECO:0000312|EMBL:EFV64284.1};
OS Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=909420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H44/76;
RX PubMed=21378179; DOI=10.1128/jb.01331-10;
RA Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA van de Beek D., Pannekoek Y., van der Ende A.;
RT "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL J. Bacteriol. 193:2371-2372(2011).
RN [2] {ECO:0007744|PDB:5WXI, ECO:0007744|PDB:5WXJ, ECO:0007744|PDB:5WXK, ECO:0007744|PDB:5XVR}
RP X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) IN COMPLEX WITH
RP DTDP-BETA-L-RHAMNOSE; DTDP AND EFP, FUNCTION, CATALYTIC ACTIVITY, ACTIVE
RP SITE, DOMAIN, AND MUTAGENESIS OF ASP-16; ASP-20; GLU-89; ASN-112; GLU-114
RP AND TYR-288.
RC STRAIN=H44/76;
RX PubMed=29440735; DOI=10.1038/s41589-018-0002-y;
RA Sengoku T., Suzuki T., Dohmae N., Watanabe C., Honma T., Hikida Y.,
RA Yamaguchi Y., Takahashi H., Yokoyama S., Yanagisawa T.;
RT "Structural basis of protein arginine rhamnosylation by glycosyltransferase
RT EarP.";
RL Nat. Chem. Biol. 14:368-374(2018).
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:29440735}.
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:29440735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66693;
CC Evidence={ECO:0000269|PubMed:29440735};
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:0000269|PubMed:29440735}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 104 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEQZ01000013; EFV64284.1; -; Genomic_DNA.
DR RefSeq; WP_002225328.1; NZ_AEQZ01000013.1.
DR PDB; 5WXI; X-ray; 2.00 A; A/B=1-382.
DR PDB; 5WXJ; X-ray; 1.85 A; A/B=1-382.
DR PDB; 5WXK; X-ray; 1.80 A; A=1-382.
DR PDB; 5XVR; X-ray; 1.63 A; A/B=1-382.
DR PDBsum; 5WXI; -.
DR PDBsum; 5WXJ; -.
DR PDBsum; 5WXK; -.
DR PDBsum; 5XVR; -.
DR AlphaFoldDB; E6MVV9; -.
DR SMR; E6MVV9; -.
DR EnsemblBacteria; EFV64284; EFV64284; NMH_0797.
DR PATRIC; fig|909420.3.peg.1694; -.
DR OMA; YFFFPGF; -.
DR BioCyc; NMEN909420:NMBH4476_RS06985-MON; -.
DR Proteomes; UP000032707; Unassembled WGS sequence.
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 3D-structure; Glycosyltransferase; Transferase.
FT CHAIN 1..382
FT /note="Protein-arginine rhamnosyltransferase"
FT /id="PRO_0000452680"
FT ACT_SITE 20
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:29440735"
FT ACT_SITE 270
FT /evidence="ECO:0000250|UniProtKB:Q9HZZ1"
FT BINDING 18..19
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXK"
FT BINDING 20
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXI, ECO:0007744|PDB:5XVR"
FT BINDING 187
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXK"
FT BINDING 187
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXI, ECO:0007744|PDB:5XVR"
FT BINDING 250..252
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXK"
FT BINDING 250..252
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXI, ECO:0007744|PDB:5XVR"
FT BINDING 268..272
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXK"
FT BINDING 268..272
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:29440735,
FT ECO:0007744|PDB:5WXI, ECO:0007744|PDB:5XVR"
FT MUTAGEN 16
FT /note="D->A: Strongly reduced protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT MUTAGEN 16
FT /note="D->N: Does not affect protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT MUTAGEN 20
FT /note="D->A,N: Abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT MUTAGEN 89
FT /note="E->A: Abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT MUTAGEN 112
FT /note="N->A: Does not affect protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT MUTAGEN 114
FT /note="E->A: Abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT MUTAGEN 288
FT /note="Y->A: Strongly reduced protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:29440735"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5XVR"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 46..52
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5WXJ"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 135..140
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 165..171
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 206..210
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:5XVR"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 262..268
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 271..279
FT /evidence="ECO:0007829|PDB:5XVR"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 333..345
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:5XVR"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:5XVR"
SQ SEQUENCE 382 AA; 44166 MW; 8CED403CEA5D59DB CRC64;
MNTPPFVCWI FCKVIDNFGD IGVSWRLARV LHRELGWQVH LWTDDVSALR ALCPDLPDVP
CVHQDIHVRT WHSDAADIDT APVPDVVIET FACDLPENVL HIIRRHKPLW LNWEYLSAEE
SNERLHLMPS PQEGVQKYFW FMGFSEKSGG LIRERDYCEA VRFDTEALRE RLMLPEKNAS
EWLLFGYRSD VWAKWLEMWR QAGSPMTLLL AGTQIIDSLK QSGVIPQDAL QNDGDVFQTA
SVRLVKIPFV PQQDFDQLLH LADCAVIRGE DSFVRAQLAG KPFFWHIYPQ DENVHLDKLH
AFWDKAHGFY TPETVSAHRR LSDDLNGGEA LSATQRLECW QTLQQHQNGW RQGAEDWSRY
LFGQPSAPEK LAAFVSKHQK IR
