EARP_PSEPK
ID EARP_PSEPK Reviewed; 377 AA.
AC Q88LS1;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Protein-arginine rhamnosyltransferase {ECO:0000305};
DE EC=2.4.1.- {ECO:0000269|PubMed:28951478};
DE AltName: Full=EF-P arginine rhamnosyltransferase {ECO:0000303|PubMed:28951478};
GN Name=earP {ECO:0000303|PubMed:28951478};
GN OrderedLocusNames=PP_1857 {ECO:0000312|EMBL:AAN67476.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2] {ECO:0007744|PDB:5NV8}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2-377 IN COMPLEX WITH
RP DTDP-BETA-L-RHAMNOSE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, DOMAIN, ACTIVE SITES, AND MUTAGENESIS OF ASP-13; ASP-17;
RP PHE-191; TYR-193; PHE-252; GLN-255; PHE-258; ARG-271; GLU-273; ASP-274;
RP SER-275 AND TYR-291.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=28951478; DOI=10.1128/mbio.01412-17;
RA Krafczyk R., Macosek J., Jagtap P.K.A., Gast D., Wunder S., Mitra P.,
RA Jha A.K., Rohr J., Hoffmann-Roder A., Jung K., Hennig J., Lassak J.;
RT "Structural basis for EarP-mediated arginine glycosylation of translation
RT elongation factor EF-P.";
RL MBio 8:0-0(2017).
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:28951478}.
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:28951478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66693;
CC Evidence={ECO:0000269|PubMed:28951478};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53 uM for dTDP-beta-L-rhamnose {ECO:0000269|PubMed:28951478};
CC Note=kcat is 35 min(-1) with dTDP-beta-L-rhamnose substrate.
CC {ECO:0000269|PubMed:28951478};
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:28951478}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 104 family.
CC {ECO:0000305}.
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DR EMBL; AE015451; AAN67476.1; -; Genomic_DNA.
DR RefSeq; NP_744012.1; NC_002947.4.
DR RefSeq; WP_010952888.1; NC_002947.4.
DR PDB; 5NV8; X-ray; 2.29 A; A=2-377.
DR PDBsum; 5NV8; -.
DR AlphaFoldDB; Q88LS1; -.
DR BMRB; Q88LS1; -.
DR SMR; Q88LS1; -.
DR STRING; 160488.PP_1857; -.
DR EnsemblBacteria; AAN67476; AAN67476; PP_1857.
DR KEGG; ppu:PP_1857; -.
DR PATRIC; fig|160488.4.peg.1958; -.
DR eggNOG; COG4394; Bacteria.
DR HOGENOM; CLU_060250_0_0_6; -.
DR OMA; YFFFPGF; -.
DR PhylomeDB; Q88LS1; -.
DR BioCyc; PPUT160488:G1G01-1961-MON; -.
DR Proteomes; UP000000556; 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..377
FT /note="Protein-arginine rhamnosyltransferase"
FT /id="PRO_0000452682"
FT ACT_SITE 17
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:28951478"
FT ACT_SITE 273
FT /evidence="ECO:0000269|PubMed:28951478"
FT BINDING 15
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:28951478,
FT ECO:0007744|PDB:5NV8"
FT BINDING 193
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:28951478,
FT ECO:0007744|PDB:5NV8"
FT BINDING 255
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:28951478,
FT ECO:0007744|PDB:5NV8"
FT BINDING 271..275
FT /ligand="dTDP-beta-L-rhamnose"
FT /ligand_id="ChEBI:CHEBI:57510"
FT /evidence="ECO:0000269|PubMed:28951478,
FT ECO:0007744|PDB:5NV8"
FT MUTAGEN 13
FT /note="D->A: Abolished protein-arginine
FT rhamnosyltransferase activity without affecting substrate-
FT binding."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 13
FT /note="D->E: Strongly reduced protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 17
FT /note="D->E,A: Abolished protein-arginine
FT rhamnosyltransferase activity without affecting substrate-
FT binding."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 191
FT /note="F->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 193
FT /note="Y->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 252
FT /note="F->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 255
FT /note="Q->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 258
FT /note="F->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 271
FT /note="R->A: Strongly reduced protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 273
FT /note="E->D: Strongly reduced protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 273
FT /note="E->Q,A: Abolished protein-arginine
FT rhamnosyltransferase activity without affecting substrate-
FT binding."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 274
FT /note="D->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 275
FT /note="S->A: Reduced protein-arginine rhamnosyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT MUTAGEN 291
FT /note="Y->A: Strongly reduced protein-arginine
FT rhamnosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:28951478"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5NV8"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 167..176
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 198..207
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 212..219
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 222..229
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 274..282
FT /evidence="ECO:0007829|PDB:5NV8"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 302..309
FT /evidence="ECO:0007829|PDB:5NV8"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 315..330
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 345..360
FT /evidence="ECO:0007829|PDB:5NV8"
FT HELIX 365..374
FT /evidence="ECO:0007829|PDB:5NV8"
SQ SEQUENCE 377 AA; 42150 MW; CC3575AD1E26B155 CRC64;
MKATWDIFCS VVDNYGDIGV TWRLARQLVA EHGLAVRLWV DDLNAFTPMC PGADATAAQQ
WQHGVDVRHW PAAWLPVAPA DVVIGAFACQ LPAAYVEAMR ARPQPPLWLN LEYLSAEDWV
EGCHGLPSPQ PNGLRKVFFF PGFTDKTGGL LREGSLLARR DGFQQSAEAR RAFLQGLGVD
LVPGALLISL FAYENPQLGN WLDALATADQ PCHLLVPQGR VVAGLSQWLG EGPLHVGDVR
TRGALTVQVL PFVSQDDFDR LLWSCDFNAV RGEDSFVRAQ WAGQPMLWHI YVQDENAHWE
KLEAFLAHYR CGLSDDADAA LLGLWRAWNM DFDMGQAWRA ARQHWPELQQ HARLWGARQA
AQPDLATALV HFYRNSL
