EFP_PSEAE
ID EFP_PSEAE Reviewed; 188 AA.
AC Q9HZZ2;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Elongation factor P {ECO:0000255|HAMAP-Rule:MF_00141};
DE Short=EF-P {ECO:0000255|HAMAP-Rule:MF_00141};
GN Name=efp {ECO:0000255|HAMAP-Rule:MF_00141}; OrderedLocusNames=PA2851;
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 GLYCOSYLATION AT ARG-32, AND MUTAGENESIS OF ARG-32.
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 GLYCOSYLATION AT ARG-32.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=28451135; DOI=10.1039/c6sc02889f;
RA Li X., Krafczyk R., Macosek J., Li Y.L., Zou Y., Simon B., Pan X., Wu Q.Y.,
RA Yan F., Li S., Hennig J., Jung K., Lassak J., Hu H.G.;
RT "Resolving the alpha-glycosidic linkage of arginine-rhamnosylated
RT translation elongation factor P triggers generation of the first ArgRha
RT specific antibody.";
RL Chem. Sci. 7:6995-7001(2016).
RN [4]
RP GLYCOSYLATION AT ARG-32.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=28451332; DOI=10.1039/c6sc03847f;
RA Wang S., Corcilius L., Sharp P.P., Rajkovic A., Ibba M., Parker B.L.,
RA Payne R.J.;
RT "Synthesis of rhamnosylated arginine glycopeptides and determination of the
RT glycosidic linkage in bacterial elongation factor P.";
RL Chem. Sci. 8:2296-2302(2017).
RN [5] {ECO:0007744|PDB:3OYY}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=21365687; DOI=10.1002/prot.22992;
RA Choi S., Choe J.;
RT "Crystal structure of elongation factor P from Pseudomonas aeruginosa at
RT 1.75 A resolution.";
RL Proteins 79:1688-1693(2011).
RN [6] {ECO:0007744|PDB:6J7M}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH EARP, GLYCOSYLATION
RP AT ARG-32, AND MUTAGENESIS OF LYS-29; THR-52 AND LYS-55.
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: Involved in peptide bond synthesis. Stimulates efficient
CC translation and peptide-bond synthesis on native or reconstituted 70S
CC ribosomes in vitro. Probably functions indirectly by altering the
CC affinity of the ribosome for aminoacyl-tRNA, thus increasing their
CC reactivity as acceptors for peptidyl transferase. {ECO:0000255|HAMAP-
CC Rule:MF_00141}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- PTM: Glycosylated ar Arg-32 by EarP: arginine rhamnosylation is
CC required for EF-P function and rescue of polyproline stalled ribosomes.
CC {ECO:0000269|PubMed:31010899}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR EMBL; AE004091; AAG06239.1; -; Genomic_DNA.
DR PIR; F83290; F83290.
DR RefSeq; NP_251541.1; NC_002516.2.
DR RefSeq; WP_003090942.1; NZ_QZGE01000011.1.
DR PDB; 3OYY; X-ray; 1.75 A; A/B=1-188.
DR PDB; 6J7M; X-ray; 2.30 A; M/N=1-188.
DR PDBsum; 3OYY; -.
DR PDBsum; 6J7M; -.
DR AlphaFoldDB; Q9HZZ2; -.
DR SMR; Q9HZZ2; -.
DR STRING; 287.DR97_5090; -.
DR PaxDb; Q9HZZ2; -.
DR PRIDE; Q9HZZ2; -.
DR EnsemblBacteria; AAG06239; AAG06239; PA2851.
DR GeneID; 882605; -.
DR KEGG; pae:PA2851; -.
DR PATRIC; fig|208964.12.peg.2991; -.
DR PseudoCAP; PA2851; -.
DR HOGENOM; CLU_074944_2_1_6; -.
DR InParanoid; Q9HZZ2; -.
DR OMA; WSVVEFQ; -.
DR PhylomeDB; Q9HZZ2; -.
DR BioCyc; PAER208964:G1FZ6-2900-MON; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR CDD; cd04470; S1_EF-P_repeat_1; 1.
DR CDD; cd05794; S1_EF-P_repeat_2; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_00141; EF_P; 1.
DR InterPro; IPR015365; Elong-fact-P_C.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR020599; Transl_elong_fac_P/YeiP.
DR InterPro; IPR013185; Transl_elong_KOW-like.
DR InterPro; IPR001059; Transl_elong_P/YeiP_cen.
DR InterPro; IPR011768; Transl_elongation_fac_P.
DR InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR PANTHER; PTHR30053; PTHR30053; 1.
DR Pfam; PF01132; EFP; 1.
DR Pfam; PF08207; EFP_N; 1.
DR Pfam; PF09285; Elong-fact-P_C; 1.
DR PIRSF; PIRSF005901; EF-P; 1.
DR SMART; SM01185; EFP; 1.
DR SMART; SM00841; Elong-fact-P_C; 1.
DR SUPFAM; SSF50104; SSF50104; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR TIGRFAMs; TIGR00038; efp; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; Glycoprotein;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..188
FT /note="Elongation factor P"
FT /id="PRO_0000094310"
FT CARBOHYD 32
FT /note="N-alpha-linked (Rha) arginine"
FT /evidence="ECO:0000269|PubMed:26060278,
FT ECO:0000269|PubMed:28451135, ECO:0000269|PubMed:28451332,
FT ECO:0000269|PubMed:31010899"
FT MUTAGEN 29
FT /note="K->A: Slightly decreased binding to EarP."
FT /evidence="ECO:0000269|PubMed:31010899"
FT MUTAGEN 32
FT /note="R->A: Abolished arginine rhamnosylation."
FT /evidence="ECO:0000269|PubMed:26060278"
FT MUTAGEN 52
FT /note="T->V: Slightly decreased binding to EarP."
FT /evidence="ECO:0000269|PubMed:31010899"
FT MUTAGEN 55
FT /note="K->A: Strongly decreased binding to EarP."
FT /evidence="ECO:0000269|PubMed:31010899"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:3OYY"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3OYY"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3OYY"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:3OYY"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 128..137
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 172..176
FT /evidence="ECO:0007829|PDB:3OYY"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:3OYY"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3OYY"
SQ SEQUENCE 188 AA; 20985 MW; 245AF4EB8811CEA1 CRC64;
MKTAQEFRAG QVANINGAPW VIQKAEFNKS GRNAAVVKMK LKNLLTGAGT ETVFKADDKL
EPIILDRKEV TYSYFADPLY VFMDSEFNQY EIEKDDLEGV LTFIEDGMTD ICEAVFYNDK
VISVELPTTI VRQIAYTEPA VRGDTSGKVM KTARLNNGAE LQVSAFCEIG DSIEIDTRTG
EYKSRVKA
