ID EFP_MARMS Reviewed; 191 AA.
AC A6VTQ2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
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=Mmwyl1_0899;
OS Marinomonas sp. (strain MWYL1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=400668;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MWYL1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA Richardson P.;
RT "Complete sequence of Marinomonas sp. MWYL1.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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: May be 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 (if this protein is present).
CC Lysylation is critical for the stimulatory effect of EF-P on peptide-
CC bond formation. The lysylation moiety may extend toward the
CC peptidyltransferase center and stabilize the terminal 3-CCA end of the
CC tRNA. Hydroxylation of the C5 position on Lys-34 may allow additional
CC potential stabilizing hydrogen-bond interactions with the P-tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
CC -!- SIMILARITY: Belongs to the elongation factor P family.
CC {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR EMBL; CP000749; ABR69831.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VTQ2; -.
DR SMR; A6VTQ2; -.
DR STRING; 400668.Mmwyl1_0899; -.
DR KEGG; mmw:Mmwyl1_0899; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_0_6; -.
DR OrthoDB; 9801844at2; -.
DR UniPathway; UPA00345; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
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; Nucleic acid-binding proteins; 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_uL2_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 NCBIfam; TIGR00038; efp; 1.
DR PANTHER; PTHR30053; ELONGATION FACTOR P; 1.
DR PANTHER; PTHR30053:SF12; ELONGATION FACTOR P (EF-P) FAMILY PROTEIN; 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; SSF50249; Nucleic acid-binding proteins; 2.
DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
DR PROSITE; PS01275; EFP; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Hydroxylation; Protein biosynthesis.
FT CHAIN 1..191
FT /note="Elongation factor P"
FT /id="PRO_1000076518"
FT MOD_RES 34
FT /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
SQ SEQUENCE 191 AA; 21013 MW; 1A697E3937C37FC0 CRC64;
MANISTSEMR SGSKVMVDGD PCAIIDNEHV KPGKGQAFNR IKLRNLKTGR VWERTFKSGD
TLETADVMDT DMEYLYTDGE FWHFMAVDGS FEQHAADETA VGDTIKWLKE QEKYVVTLYN
GAPLAVAAPN FIELEVKETD PGVKGDTANG GSKPAFLVTG AMVRVPLFIN IGEVLRVDTR
TGEYVSRATG K
//
