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Database: UniProt
Entry: A0A090AD47_9GAMM
LinkDB: A0A090AD47_9GAMM
Original site: A0A090AD47_9GAMM 
ID   A0A090AD47_9GAMM        Unreviewed;       189 AA.
AC   A0A090AD47;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Elongation factor P {ECO:0000256|HAMAP-Rule:MF_00141};
DE            Short=EF-P {ECO:0000256|HAMAP-Rule:MF_00141};
GN   Name=efp {ECO:0000256|HAMAP-Rule:MF_00141};
GN   ORFNames=THII_0417 {ECO:0000313|EMBL:BAP54714.1};
OS   Thioploca ingrica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thioploca.
OX   NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP54714.1, ECO:0000313|Proteomes:UP000031623};
RN   [1] {ECO:0000313|EMBL:BAP54714.1, ECO:0000313|Proteomes:UP000031623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA   Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT   "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT   sequence supplemented with proteomic evidence.";
RL   ISME J. 0:0-0(2014).
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:0000256|HAMAP-Rule:MF_00141}.
CC   -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC       {ECO:0000256|ARBA:ARBA00004815, ECO:0000256|HAMAP-Rule:MF_00141}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|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:0000256|HAMAP-Rule:MF_00141}.
CC   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000256|ARBA:ARBA00009479, ECO:0000256|HAMAP-Rule:MF_00141,
CC       ECO:0000256|RuleBase:RU004389}.
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DR   EMBL; AP014633; BAP54714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090AD47; -.
DR   STRING; 40754.THII_0417; -.
DR   KEGG; tig:THII_0417; -.
DR   HOGENOM; CLU_074944_0_0_6; -.
DR   OrthoDB; 9801844at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000031623; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00141};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00141};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278, ECO:0000256|HAMAP-
KW   Rule:MF_00141};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00141}; Reference proteome {ECO:0000313|Proteomes:UP000031623}.
FT   DOMAIN          69..123
FT                   /note="Translation elongation factor P/YeiP central"
FT                   /evidence="ECO:0000259|SMART:SM01185"
FT   DOMAIN          131..186
FT                   /note="Elongation factor P C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00841"
FT   MOD_RES         34
FT                   /note="N6-(3,6-diaminohexanoyl)-5-hydroxylysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00141"
SQ   SEQUENCE   189 AA;  20704 MW;  88120EA4E6831E52 CRC64;
     MAVFSTNEFK SGLKLMIDGD PCSIIENEFV KPGKGQAFSR VKFRNLKTGR VIERTFKSGD
     TAEGADVVET NMEYLYNDGE FFHFMVTDTY EQYAASNAAV GDSVKWLKGQ EKCIITLWNN
     DPIAVTPPNF VVLAVTDTEP GVRGDTSSGG SKPATLETGA TVRVPLFVNV GDLIKVDTRT
     GEYLSRAKE
//
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