ID A0A2S8SSE9_9BACT Unreviewed; 215 AA.
AC A0A2S8SSE9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=B1R32_10971 {ECO:0000313|EMBL:PQV63731.1};
OS Abditibacterium utsteinense.
OC Bacteria; Abditibacteriota; Abditibacteriia; Abditibacteriales;
OC Abditibacteriaceae; Abditibacterium.
OX NCBI_TaxID=1960156 {ECO:0000313|EMBL:PQV63731.1, ECO:0000313|Proteomes:UP000237684};
RN [1] {ECO:0000313|EMBL:PQV63731.1, ECO:0000313|Proteomes:UP000237684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29911 {ECO:0000313|EMBL:PQV63731.1,
RC ECO:0000313|Proteomes:UP000237684};
RX PubMed=29475572;
RA Tahon G., Tytgat B., Lebbe L., Carlier A., Willems A.;
RT "Abditibacterium utsteinense sp. nov., the first cultivated member of
RT candidate phylum FBP, isolated from ice-free Antarctic soil samples.";
RL Syst. Appl. Microbiol. 0:0-0(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: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}.
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:PQV63731.1}.
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DR EMBL; NIGF01000009; PQV63731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S8SSE9; -.
DR InParanoid; A0A2S8SSE9; -.
DR OrthoDB; 9801844at2; -.
DR UniPathway; UPA00345; -.
DR Proteomes; UP000237684; 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:UP000237684}.
FT DOMAIN 96..150
FT /note="Translation elongation factor P/YeiP central"
FT /evidence="ECO:0000259|SMART:SM01185"
FT DOMAIN 158..213
FT /note="Elongation factor P C-terminal"
FT /evidence="ECO:0000259|SMART:SM00841"
SQ SEQUENCE 215 AA; 23934 MW; 71585E2CF422DDEA CRC64;
MISGEIIPPQ IPCFAVLKFQ KTVIGASLVA LSTADFKNGL TLEYEGKVFQ ILEFQHVKPG
KGGAFVRSKL RNLQTGATVE KTWRAGDSME AALVERRNVE FLYRDGDDLN FMDMQDFEPM
QMPAKVVGDV AKFLKDNTTV QLMTWKDIVL SVELPQSMEY VITQTDPGFR GDTVQGGTKP
ATIETGAQIN VPMFVNEGDM IKVDTRTGTY LERVK
//
