EARP_PSEAE
ID EARP_PSEAE Reviewed; 376 AA.
AC Q9HZZ1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein-arginine rhamnosyltransferase {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:31010899, ECO:0000305|PubMed:26060278};
DE AltName: Full=EF-P arginine rhamnosyltransferase {ECO:0000303|PubMed:26060278};
GN Name=earP {ECO:0000303|PubMed:26060278};
GN OrderedLocusNames=PA2852 {ECO:0000312|EMBL:AAG06240.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=26060278; DOI=10.1128/mbio.00823-15;
RA Rajkovic A., Erickson S., Witzky A., Branson O.E., Seo J., Gafken P.R.,
RA Frietas M.A., Whitelegge J.P., Faull K.F., Navarre W., Darwin A.J.,
RA Ibba M.;
RT "Cyclic rhamnosylated elongation factor P establishes antibiotic resistance
RT in Pseudomonas aeruginosa.";
RL MBio 6:e00823-e00823(2015).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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).
RN [4] {ECO:0007744|PDB:6J7J, ECO:0007744|PDB:6J7K, ECO:0007744|PDB:6J7L}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH
RP DTDP-BETA-L-RHAMNOSE; DTDP AND EFP, FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
RP ACTIVE SITES, AND MUTAGENESIS OF ASP-12; ASP-16; TYR-112 AND GLU-272.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31010899; DOI=10.1128/jb.00128-19;
RA He C., Liu N., Li F., Jia X., Peng H., Liu Y., Xiao Y.;
RT "Complex structure of Pseudomonas aeruginosa arginine rhamnosyltransferase
RT EarP with its acceptor elongation factor P.";
RL J. Bacteriol. 201:0-0(2019).
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:26060278,
CC ECO:0000269|PubMed:31010899}.
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:31010899, ECO:0000305|PubMed:26060278};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66693;
CC Evidence={ECO:0000269|PubMed:31010899, ECO:0000305|PubMed:26060278};
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:31010899}.
CC -!- DISRUPTION PHENOTYPE: Reduced bacterial fitness and reduced
CC pathogenicity. {ECO:0000269|PubMed:25686373}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 104 family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG06240.1; -; Genomic_DNA.
DR PIR; G83290; G83290.
DR RefSeq; NP_251542.1; NC_002516.2.
DR RefSeq; WP_003114754.1; NZ_QZGE01000011.1.
DR PDB; 6J7J; X-ray; 1.75 A; A=1-376.
DR PDB; 6J7K; X-ray; 2.15 A; A=1-376.
DR PDB; 6J7L; X-ray; 1.85 A; A=1-376.
DR PDB; 6J7M; X-ray; 2.30 A; A/C=1-376.
DR PDBsum; 6J7J; -.
DR PDBsum; 6J7K; -.
DR PDBsum; 6J7L; -.
DR PDBsum; 6J7M; -.
DR AlphaFoldDB; Q9HZZ1; -.
DR SMR; Q9HZZ1; -.
DR STRING; 287.DR97_5089; -.
DR PaxDb; Q9HZZ1; -.
DR PRIDE; Q9HZZ1; -.
DR EnsemblBacteria; AAG06240; AAG06240; PA2852.
DR GeneID; 882634; -.
DR KEGG; pae:PA2852; -.
DR PATRIC; fig|208964.12.peg.2992; -.
DR PseudoCAP; PA2852; -.
DR HOGENOM; CLU_060250_0_0_6; -.
DR InParanoid; Q9HZZ1; -.
DR OMA; YFFFPGF; -.
DR PhylomeDB; Q9HZZ1; -.
DR BioCyc; PAER208964:G1FZ6-2901-MON; -.
DR Proteomes; UP000002438; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..376
FT /note="Protein-arginine rhamnosyltransferase"
FT /id="PRO_0000452681"
FT REGION 252..254
FT /note="dTDP-beta-L-rhamnose"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7K"
FT ACT_SITE 16
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:31010899"
FT ACT_SITE 272
FT /evidence="ECO:0000269|PubMed:31010899"
FT BINDING 13..16
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7K"
FT BINDING 14..15
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M"
FT BINDING 192
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M"
FT BINDING 192
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7K"
FT BINDING 252..254
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M"
FT BINDING 270..274
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7L, ECO:0007744|PDB:6J7M"
FT BINDING 270..274
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:31010899,
FT ECO:0007744|PDB:6J7K"
FT MUTAGEN 12
FT /note="D->N: Decreased but not abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31010899"
FT MUTAGEN 16
FT /note="D->N: Abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31010899"
FT MUTAGEN 112
FT /note="Y->F: Decreased but not abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31010899"
FT MUTAGEN 272
FT /note="E->Q: Abolished protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:31010899"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:6J7L"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 254..263
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 272..280
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:6J7J"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:6J7K"
FT HELIX 298..309
FT /evidence="ECO:0007829|PDB:6J7J"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6J7M"
FT HELIX 314..329
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 334..341
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:6J7J"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:6J7J"
SQ SEQUENCE 376 AA; 42787 MW; BFCA969AB74739C2 CRC64;
MASWDIFCSV VDNYGDIGVT WRLARQLAAE HGQAVRLWVD EPQAFARICP RADPVAHVQC
LDGVEVRAWG RPWAPVAAAD VVIEAFACEL PEAHRQAMRE RKRPSLWLNL EYLSAEEWIG
SCHALPSLQA CGLSKYFFFP GFREPSGGLL REAGLLERRR RFQASVSAQD EFLASLGVRR
KVGERLISLF AYENPALPGW LEQLRDARQP SLLLVPEGRV LADVADWLRV ATLAVGDVHV
RDALRVQVLP FMAQDDYDRL LWCCDLNAVR GEDSFVRAQW AGRPLLWHIY RQEEETHLAK
LEAFLELYCA GLPADLAENL RTFWLAWNAG GGLAGAWEGL ERQLPEWRRE AQRWADEQGM
RPDLAARLVQ FYADWL
