ID U2TJH4_STRPY Unreviewed; 613 AA. AC U2TJH4; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 13-SEP-2023, entry version 41. 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=typA {ECO:0000313|EMBL:ERL06625.1}; GN Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849}; GN ORFNames=HMPREF1231_2118 {ECO:0000313|EMBL:ERL06625.1}; OS Streptococcus pyogenes GA06023. OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=1115816 {ECO:0000313|EMBL:ERL06625.1, ECO:0000313|Proteomes:UP000016663}; RN [1] {ECO:0000313|EMBL:ERL06625.1, ECO:0000313|Proteomes:UP000016663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GA06023 {ECO:0000313|EMBL:ERL06625.1, RC ECO:0000313|Proteomes:UP000016663}; RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H., RA Methe B., Sutton G., Nelson K.E.; RL Submitted (SEP-2013) 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 -!- 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:ERL06625.1}. 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; AWPJ01000416; ERL06625.1; -; Genomic_DNA. DR AlphaFoldDB; U2TJH4; -. DR EnsemblBacteria; ERL06625; ERL06625; HMPREF1231_2118. DR PATRIC; fig|1115816.3.peg.2005; -. DR Proteomes; UP000016663; 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; cd16263; BipA_III; 1. DR CDD; cd03710; BipA_TypA_C; 1. DR CDD; cd03691; BipA_TypA_II; 1. DR CDD; cd01891; TypA_BipA; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 2.40.50.250; bipa protein; 1. DR Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 1. DR HAMAP; MF_00849; BipA; 1. DR InterPro; IPR006298; BipA. DR InterPro; IPR047041; BipA_GTP-bd_dom. DR InterPro; IPR047042; BipA_II. DR InterPro; IPR047043; BipA_III. 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 NCBIfam; TIGR00231; small_GTP; 1. DR NCBIfam; TIGR01394; TypA_BipA; 1. DR PANTHER; PTHR42908:SF8; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR42908; TRANSLATION ELONGATION FACTOR-RELATED; 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; SSF54980; EF-G C-terminal domain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 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 6..203 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 18..23 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" FT BINDING 131..134 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" SQ SEQUENCE 613 AA; 68573 MW; 099B4958C19A481D CRC64; MTNLRNDIRN VAIIAHVDHG KTTLVDELLK QSHTLDERKE LQERAMDSND LEKERGITIL AKNTAVAYND VRINIMDTPG HADFGGEVER IMKMVDGVVL VVDAYEGTMP QTRFVLKKAL EQNLIPIVVV NKIDKPSARP AEVVDEVLEL FIELGADDEQ LEFPVVYASA INGTSSLSDD PADQEHTMAP IFDTIIDHIP APVDNSDEPL QFQVSLLDYN DFVGRIGIGR VFRGTVKVGD QVTLSKLDGT TKNFRVTKLF GFFGLERREI QEAKAGDLIA VSGMEDIFVG ETITPTDCVE ALPILRIDEP TLQMTFLVNN SPFAGREGKW ITSRKVEERL LAELQTDVSL RVDPTDSPDK WTVSGRGELH LSILIETMRR EGYELQVSRP EVIIKEIDGV KCEPFERVQI DTPEEYQGAI IQSLSERKGD MLDMQMVGNG QTRLIFLIPA RGLIGYSTEF LSMTRGYGIM NHTFDQYLPV VQGEIGGRHR GALVSIENGK ATTYSIMRIE ERGTIFVNPG TEVYEGMIVG ENSRDNDLGV NITTAKQMTN VRSATKDQTA VIKTPRILTL EESLEFLNDD EYMEVTPESI RLRKQILNKA ARDKANKKKK SAE //