ID   EFP_NEIMH               Reviewed;         186 AA.
AC   E6MVW0;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 72.
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};
GN   ORFNames=NMH_0798 {ECO:0000312|EMBL:EFV64285.1};
OS   Neisseria meningitidis serogroup B / serotype 15 (strain H44/76).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=909420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H44/76;
RX   PubMed=21378179; DOI=10.1128/jb.01331-10;
RA   Piet J.R., Huis In 't Veld R.A., van Schaik B.D., van Kampen A.H., Baas F.,
RA   van de Beek D., Pannekoek Y., van der Ende A.;
RT   "Genome sequence of Neisseria meningitidis serogroup B strain H44/76.";
RL   J. Bacteriol. 193:2371-2372(2011).
RN   [2] {ECO:0007744|PDB:5WXK}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-63 IN COMPLEX WITH EARP, AND
RP   GLYCOSYLATION AT ARG-32.
RC   STRAIN=H44/76;
RX   PubMed=29440735; DOI=10.1038/s41589-018-0002-y;
RA   Sengoku T., Suzuki T., Dohmae N., Watanabe C., Honma T., Hikida Y.,
RA   Yamaguchi Y., Takahashi H., Yokoyama S., Yanagisawa T.;
RT   "Structural basis of protein arginine rhamnosylation by glycosyltransferase
RT   EarP.";
RL   Nat. Chem. Biol. 14:368-374(2018).
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:0000250|UniProtKB:P0DUK0}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000255|HAMAP-Rule:MF_00141}.
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DR   EMBL; AEQZ01000013; EFV64285.1; -; Genomic_DNA.
DR   RefSeq; WP_002219406.1; NZ_AEQZ01000013.1.
DR   PDB; 5WXK; X-ray; 1.80 A; B=1-63.
DR   PDBsum; 5WXK; -.
DR   AlphaFoldDB; E6MVW0; -.
DR   SMR; E6MVW0; -.
DR   EnsemblBacteria; EFV64285; EFV64285; NMH_0798.
DR   GeneID; 61281154; -.
DR   GeneID; 64350097; -.
DR   GeneID; 66753265; -.
DR   PATRIC; fig|909420.3.peg.1693; -.
DR   OMA; LYRMRMY; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000032707; Unassembled WGS sequence.
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; -; 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.
FT   CHAIN           1..186
FT                   /note="Elongation factor P"
FT                   /id="PRO_0000452685"
FT   CARBOHYD        32
FT                   /note="N-alpha-linked (Rha) arginine"
FT                   /evidence="ECO:0000269|PubMed:29440735"
FT   HELIX           4..6
FT                   /evidence="ECO:0007829|PDB:5WXK"
FT   STRAND          11..15
FT                   /evidence="ECO:0007829|PDB:5WXK"
FT   STRAND          18..29
FT                   /evidence="ECO:0007829|PDB:5WXK"
FT   STRAND          35..43
FT                   /evidence="ECO:0007829|PDB:5WXK"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:5WXK"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:5WXK"
SQ   SEQUENCE   186 AA;  20880 MW;  3502433BE9D8E189 CRC64;
     MKTAQELRAG NVFMVGNDPM VVQKTEYIKG GRSSAKVSMK LKNLLTGAAS ETIYKADDKF
     DVVILSRKNC TYSYFADPMY VFMDEEFNQY EIEADNIGDA LKFIVDGMED QCEVTFYEGN
     PISVELPTII VREVEYTEPA VKGDTSGKVM KTARLVGGTE IQVMSYIENG DKVEIDTRTG
     EFRKRA