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Database: UniProt
Entry: A0A147K816_9BACI
LinkDB: A0A147K816_9BACI
Original site: A0A147K816_9BACI 
ID   A0A147K816_9BACI        Unreviewed;       185 AA.
AC   A0A147K816;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=Q75_09650 {ECO:0000313|EMBL:KUP06185.1};
OS   Bacillus coahuilensis p1.1.43.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1150625 {ECO:0000313|EMBL:KUP06185.1, ECO:0000313|Proteomes:UP000074108};
RN   [1] {ECO:0000313|EMBL:KUP06185.1, ECO:0000313|Proteomes:UP000074108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=p1.1.43 {ECO:0000313|Proteomes:UP000074108};
RX   PubMed=26903955; DOI=10.3389/fmicb.2016.00058;
RA   Gomez-Lunar Z., Hernandez-Gonzalez I., Rodriguez-Torres M.D., Souza V.,
RA   Olmedo-Alvarez G.;
RT   "Microevolution Analysis of Bacillus coahuilensis Unveils Differences in
RT   Phosphorus Acquisition Strategies and Their Regulation.";
RL   Front. Microbiol. 7:58-58(2016).
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.
CC       {ECO:0000256|ARBA:ARBA00025469, 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   -!- SIMILARITY: Belongs to the elongation factor P family.
CC       {ECO:0000256|ARBA:ARBA00009479, ECO:0000256|HAMAP-Rule:MF_00141,
CC       ECO:0000256|RuleBase:RU004389}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUP06185.1}.
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DR   EMBL; LDYG01000030; KUP06185.1; -; Genomic_DNA.
DR   RefSeq; WP_010173520.1; NZ_LDYG01000030.1.
DR   AlphaFoldDB; A0A147K816; -.
DR   STRING; 1150625.Q75_09650; -.
DR   PATRIC; fig|1150625.3.peg.2052; -.
DR   OrthoDB; 9801844at2; -.
DR   UniPathway; UPA00345; -.
DR   Proteomes; UP000074108; 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; 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   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00141}; Reference proteome {ECO:0000313|Proteomes:UP000074108}.
FT   DOMAIN          67..121
FT                   /note="Translation elongation factor P/YeiP central"
FT                   /evidence="ECO:0000259|SMART:SM01185"
FT   DOMAIN          129..184
FT                   /note="Elongation factor P C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00841"
SQ   SEQUENCE   185 AA;  20470 MW;  0E2D81F5850AE341 CRC64;
     MISVNDFRTG LTIEVDNGIW RVLDFQHVKP GKGAAFVRSK LRNLRTGAIQ EKTFRAGEKV
     GKAQIDNRKM QYLYANGDMH VFMDTESYDQ IELPATSIEY ELKYLKENME VHIMMYGGET
     LGVELPNTVN LTVTETEPGI KGDTATGGSK PATVETGLIV NVPFFVNEGD VLVVNTTDGS
     YVSRG
//
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