EFP_SALTY
ID EFP_SALTY Reviewed; 188 AA.
AC P64036; Q8XFX2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
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=STM4334;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP BETA-LYSYLATION AT LYS-34 BY EPMA, AND HYDROXYLATION AT LYS-34.
RX PubMed=20670890; DOI=10.1016/j.molcel.2010.06.021;
RA Navarre W.W., Zou S.B., Roy H., Xie J.L., Savchenko A., Singer A.,
RA Edvokimova E., Prost L.R., Kumar R., Ibba M., Fang F.C.;
RT "PoxA, YjeK, and elongation factor P coordinately modulate virulence and
RT drug resistance in Salmonella enterica.";
RL Mol. Cell 39:209-221(2010).
RN [3]
RP DISRUPTION PHENOTYPE, AND ROLE IN MEMBRANE INTEGRITY.
RC STRAIN=14028s / SGSC 2262;
RX PubMed=22081389; DOI=10.1128/jb.05864-11;
RA Zou S.B., Hersch S.J., Roy H., Wiggers J.B., Leung A.S., Buranyi S.,
RA Xie J.L., Dare K., Ibba M., Navarre W.W.;
RT "Loss of elongation factor P disrupts bacterial outer membrane integrity.";
RL J. Bacteriol. 194:413-425(2012).
CC -!- FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome
CC stalling that occurs when 3 or more consecutive Pro residues or the
CC sequence PPG is present in a protein, possibly by augmenting the
CC peptidyl transferase activity of the ribosome. Modification of Lys-34
CC is required for alleviation. {ECO:0000255|HAMAP-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: Is beta-lysylated on the epsilon-amino group of Lys-34 by the
CC combined action of EpmA and EpmB, and then hydroxylated on the C5
CC position of the same residue by EpmC. Lysylation is critical for the
CC stimulatory effect of EF-P on peptide-bond formation. The lysylation
CC moiety would extend toward the peptidyltransferase center and stabilize
CC the terminal 3-CCA end of the tRNA. The hydroxylation of the C5
CC position on Lys-34 would allow additional potential stabilizing
CC hydrogen-bond interactions with the P-tRNA (Probable)
CC (PubMed:20670890). {ECO:0000269|PubMed:20670890}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking EF-P display highly pleiotropic
CC phenotypes similar to those lacking EmpA or EmpB. They exhibit reduced
CC growth rates, and they display increased susceptibility to hypoosmotic
CC conditions, antibiotics, and detergents and enhanced resistance to the
CC compound S-nitrosoglutathione. The susceptibility phenotypes are
CC largely explained by the enhanced membrane permeability of the efp
CC mutant. Analysis of the membrane proteomes of wild-type and efp mutant
CC strains reveals few changes, including the prominent overexpression of
CC a single porin, KdgM (STM1131), in the efp mutant outer membrane.
CC {ECO:0000269|PubMed:22081389}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR EMBL; AE006468; AAL23157.1; -; Genomic_DNA.
DR RefSeq; NP_463198.1; NC_003197.2.
DR RefSeq; WP_000257282.1; NC_003197.2.
DR AlphaFoldDB; P64036; -.
DR SMR; P64036; -.
DR STRING; 99287.STM4334; -.
DR PaxDb; P64036; -.
DR EnsemblBacteria; AAL23157; AAL23157; STM4334.
DR GeneID; 1255860; -.
DR GeneID; 66758562; -.
DR KEGG; stm:STM4334; -.
DR PATRIC; fig|99287.12.peg.4560; -.
DR HOGENOM; CLU_074944_0_0_6; -.
DR OMA; WSVVEFQ; -.
DR PhylomeDB; P64036; -.
DR BioCyc; SENT99287:STM4334-MON; -.
DR UniPathway; UPA00345; -.
DR PHI-base; PHI:6420; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; IPR013852; Transl_elong_P/YeiP_CS.
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.
DR PROSITE; PS01275; EFP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; Hydroxylation; Protein biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..188
FT /note="Elongation factor P"
FT /id="PRO_0000094323"
FT MOD_RES 34
FT /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00141,
FT ECO:0000269|PubMed:20670890"
SQ SEQUENCE 188 AA; 20623 MW; 76D5264BF296C790 CRC64;
MATYYSNDFR SGLKIMLDGE PYAVESSEFV KPGKGQAFAR VKLRRLLTGT RVEKTFKSTD
SAEGADVVDM NLTYLYNDGE FWHFMNNETF EQLSADAKAI GDNAKWLLDQ AECIVTLWNG
QPISVTPPNF VELEIVDTDP GLKGDTAGTG GKPATLSTGA VVKVPLFVQI GEVIKVDTRS
GEYVSRVK
