ID D4DST2_NEIEG Unreviewed; 186 AA.
AC D4DST2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 62.
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 ECO:0000313|EMBL:EFE49116.1};
GN ORFNames=NEIELOOT_02128 {ECO:0000313|EMBL:EFE49116.1}, NELON_08825
GN {ECO:0000313|EMBL:AJE18985.1};
OS Neisseria elongata subsp. glycolytica ATCC 29315.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546263 {ECO:0000313|EMBL:EFE49116.1, ECO:0000313|Proteomes:UP000005536};
RN [1] {ECO:0000313|EMBL:EFE49116.1, ECO:0000313|Proteomes:UP000005536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:EFE49116.1,
RC ECO:0000313|Proteomes:UP000005536};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392};
RA Veyrier F.J., Taha M.-K.;
RT "Complete Genome sequence of Neisseria elongata subsp. glycolytica.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AJE18985.1, ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:AJE18985.1,
RC ECO:0000313|Proteomes:UP000031392};
RX PubMed=26162030;
RA Veyrier F.J., Biais N., Morales P., Belkacem N., Guilhen C., Ranjeva S.,
RA Sismeiro O., Pehau-Arnaudet G., Rocha E.P., Werts C., Taha M.K.,
RA Boneca I.G.;
RT "Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.";
RL PLoS Genet. 11:E1005338-E1005338(2015).
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:0000256|HAMAP-
CC 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}.
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DR EMBL; CP007726; AJE18985.1; -; Genomic_DNA.
DR EMBL; ADBF01000227; EFE49116.1; -; Genomic_DNA.
DR RefSeq; WP_003773652.1; NZ_CP007726.1.
DR AlphaFoldDB; D4DST2; -.
DR STRING; 546263.NELON_08825; -.
DR KEGG; nel:NELON_08825; -.
DR PATRIC; fig|546263.7.peg.1898; -.
DR HOGENOM; CLU_074944_2_1_4; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000005536; Unassembled WGS sequence.
DR Proteomes; UP000031392; 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 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; 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.
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:UP000031392}.
FT DOMAIN 67..122
FT /note="Translation elongation factor P/YeiP central"
FT /evidence="ECO:0000259|SMART:SM01185"
FT DOMAIN 130..185
FT /note="Elongation factor P C-terminal"
FT /evidence="ECO:0000259|SMART:SM00841"
SQ SEQUENCE 186 AA; 20848 MW; 821AFA5A9E8A8C46 CRC64;
MKTAQELRAG NVFMVGNDPM VVQKTEYIKG GRSSAKVSMK LKNLLTGAAS ENIYKADDKF
DVVILARKNC TYSYFADPMY VFMDEEFNQY EIEADNIGDA LKFIVEGMED VCEVTFYEGN
PISVELPTII VREVEYTEPA VKGDTSGKVM KTARLVGGTE IQVMSYVENG DKVEIDTRTG
EFRKRA
//
