ID A0A7U8ID74_ENTFC Unreviewed; 623 AA. AC A0A7U8ID74; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 03-AUG-2022, entry version 5. DE RecName: Full=50S ribosomal subunit assembly factor BipA {ECO:0000256|HAMAP-Rule:MF_00849}; DE EC=3.6.5.- {ECO:0000256|HAMAP-Rule:MF_00849}; DE AltName: Full=GTP-binding protein BipA {ECO:0000256|HAMAP-Rule:MF_00849}; GN Name=bipA {ECO:0000256|HAMAP-Rule:MF_00849}; GN ORFNames=EFQG_00237 {ECO:0000313|EMBL:EEV44089.1}; OS Enterococcus faecium 1,231,502. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=565657 {ECO:0000313|EMBL:EEV44089.1}; RN [1] {ECO:0000313|EMBL:EEV44089.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1 {ECO:0000313|EMBL:EEV44089.1}; RG The Broad Institute Genome Sequencing Platform; RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A., RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., RA White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K., RA Lander E., Nusbaum C., Galagan J., Birren B.; RT "The Genome Sequence of Enterococcus faecium strain 1,231,502."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: A 50S ribosomal subunit assembly protein with GTPase CC activity, required for 50S subunit assembly at low temperatures, may CC also play a role in translation. Binds GTP and analogs. Binds the 70S CC ribosome between the 30S and 50S subunits, in a similar position as CC ribosome-bound EF-G; it contacts a number of ribosomal proteins, both CC rRNAs and the A-site tRNA. {ECO:0000256|HAMAP-Rule:MF_00849}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00849}; CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00849}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00849}. CC Note=Binds to ribosomes. {ECO:0000256|HAMAP-Rule:MF_00849}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. BipA subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00849}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG688486; EEV44089.1; -; Genomic_DNA. DR Proteomes; UP000004657; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR CDD; cd03710; BipA_TypA_C; 1. DR Gene3D; 2.40.50.250; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00849; BipA; 1. DR InterPro; IPR035651; BipA_V. DR InterPro; IPR035647; EFG_III/V. DR InterPro; IPR000640; EFG_V-like. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR042116; TypA/BipA_C. DR InterPro; IPR006298; TypA_GTP-bd. DR PANTHER; PTHR42908:SF8; PTHR42908:SF8; 1. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR TIGRFAMs; TIGR01394; TypA_BipA; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00849}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00849}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00849}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00849}; Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}; KW Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00849}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00849}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00849}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00849}. FT DOMAIN 19..216 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 31..36 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" FT BINDING 144..147 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" SQ SEQUENCE 623 AA; 69674 MW; 3CB7C13D2FDB5CA8 CRC64; MPCHKEPIKK ELVTLNYRND IRNVAIIAHV DHGKTTLVDE LLKQSDTLDA HTQLQERAMD SNALEKERGI TILAKNTAVD YKGIRVNIMD TPGHADFGGE VERIMKMVDG VVLVVDAYEG TMPQTRFVLK KALEQHITPI VVVNKIDKPS ARPEHVVDEV LELFIELGAD DDQLDFPVIY ASALNGTSSL SDDPADQEPT MAPIFDTIIE KIPAPVDNSD EPLQFQVSLL DYNDYVGRIG IGRVFRGTIK VGDQVALIKL DGTVKKFRVT KLFGFFGLKR LEIQEAKAGD LIAVSGMEDI FVGETVTPVD HQDALPILHI DEPTLQMTFL VNNSPFAGRE GKFVTARKIE ERLMAELQTD VSLRVEPTNS PDAWTVSGRG ELHLSILIEN MRREGYELQV SRPEVIEKEI DGVKCEPFER VQIDTPEEYM GSVIESLSLR KGEMQDMVHT GNGQIRLTFL TPARGLIGYS TEFLSMTRGY GIMNHTFDQY LPMLPGQIGG RHQGALVSID TGKATTYSIM SIEERGTVFV EPGTEVYEGM IIGENSRDND LTVNITKAKQ MTNVRSATKD QTSVIKKPKQ LTLEESLEFL NDDEYCEVTP ESIRLRKQIL EKNAREKASK KKK //