EFP_COXBU
ID EFP_COXBU Reviewed; 188 AA.
AC Q83AR4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=CBU_1816;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO91309.1; -; Genomic_DNA.
DR RefSeq; NP_820795.1; NC_002971.3.
DR RefSeq; WP_005772139.1; NZ_CDBG01000001.1.
DR PDB; 3TRE; X-ray; 2.90 A; A=1-188.
DR PDBsum; 3TRE; -.
DR AlphaFoldDB; Q83AR4; -.
DR SMR; Q83AR4; -.
DR STRING; 227377.CBU_1816; -.
DR DNASU; 1209727; -.
DR EnsemblBacteria; AAO91309; AAO91309; CBU_1816.
DR GeneID; 1209727; -.
DR KEGG; cbu:CBU_1816; -.
DR PATRIC; fig|227377.7.peg.1802; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_0_6; -.
DR OMA; WSVVEFQ; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000002671; 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 DisProt; DP01015; -.
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 3D-structure; Cytoplasm; Elongation factor; Hydroxylation;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..188
FT /note="Elongation factor P"
FT /id="PRO_0000094241"
FT MOD_RES 34
FT /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00141"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 20..30
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:3TRE"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 67..77
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:3TRE"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:3TRE"
FT HELIX 101..106
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 112..118
FT /evidence="ECO:0007829|PDB:3TRE"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3TRE"
SQ SEQUENCE 188 AA; 21045 MW; CA879258AFAE41E3 CRC64;
MATHSTNEFR GGLKVMVDGD PCSIIDNEFV KPGKGQAFNR VKFRNLKTGR VLERTFKSGE
TLPAADVVEV EMQYLYNDGE FWHFMTSENY EQHAASKEAV AEAKQWLKEE ALCMVTMWNG
VPLSVEPPNF VELKITETEP GVRGDTATGG TKRAKLETGA VVRVPLFLNE GEIIKVDTRR
GEYVSRAK
