EFP_CORGL
ID EFP_CORGL Reviewed; 187 AA.
AC Q45288;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Elongation factor P;
DE Short=EF-P;
GN Name=efp; OrderedLocusNames=Cgl1619, cg1825;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13869 / DSMZ 1412 / NCIMB 9567;
RX PubMed=9370284; DOI=10.1016/s0378-1119(97)00317-x;
RA Ramos A., Macias J.R., Gil J.A.;
RT "Cloning, sequencing and expression of the gene encoding elongation factor
RT P in the amino-acid producer Brevibacterium lactofermentum (Corynebacterium
RT glutamicum ATCC 13869).";
RL Gene 198:217-222(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 (By similarity).
CC {ECO:0000250}.
CC -!- PATHWAY: Protein biosynthesis; polypeptide chain elongation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the elongation factor P family. {ECO:0000305}.
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DR EMBL; X99289; CAA67673.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99012.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21628.1; -; Genomic_DNA.
DR RefSeq; NP_600833.1; NC_003450.3.
DR RefSeq; WP_003855973.1; NC_006958.1.
DR PDB; 6S8Z; X-ray; 2.20 A; A=1-187.
DR PDBsum; 6S8Z; -.
DR AlphaFoldDB; Q45288; -.
DR SMR; Q45288; -.
DR STRING; 196627.cg1825; -.
DR World-2DPAGE; 0001:Q45288; -.
DR GeneID; 58309196; -.
DR KEGG; cgb:cg1825; -.
DR KEGG; cgl:Cgl1619; -.
DR PATRIC; fig|196627.13.peg.1581; -.
DR eggNOG; COG0231; Bacteria.
DR HOGENOM; CLU_074944_0_1_11; -.
DR OMA; WSVVEFQ; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000000582; Chromosome.
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; 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; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..187
FT /note="Elongation factor P"
FT /id="PRO_0000094240"
FT CONFLICT 68..70
FT /note="RDV -> PRC (in Ref. 1; CAA67673)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:6S8Z"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6S8Z"
FT TURN 85..87
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6S8Z"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:6S8Z"
FT HELIX 99..104
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:6S8Z"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:6S8Z"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:6S8Z"
SQ SEQUENCE 187 AA; 20640 MW; 8860822582C6A849 CRC64;
MATTADFKNG LVLKNEGKLQ QIIEFQHVKP GKGPAFVRTK LKDVVTGKTI DKTWNAGVKV
ETATVDRRDV TYLYNDGTSF IVMDDKTFEQ YELSPDAFGD AGRFLLENMR VQVSFHEGEA
LFGELPVSVD LRVEHTDPGL QGDRSTGGTK PATLETGAEI QVPLFIETGN VLKVDTRDGS
YLSRVNN
