ID D9Q9M3_CORP2 Unreviewed; 636 AA. AC D9Q9M3; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-NOV-2024, entry version 77. DE RecName: Full=Large 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:ADL10249.1}; GN Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849}; GN ORFNames=CPC231_03855 {ECO:0000313|EMBL:ADL10249.1}; OS Corynebacterium pseudotuberculosis (strain C231). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10249.1, ECO:0000313|Proteomes:UP000000276}; RN [1] {ECO:0000313|EMBL:ADL10249.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10249.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21037006; DOI=.1128/JB.01211-10; RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP); RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T., RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S., RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F., RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.; RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a RT strain isolated from a cow in Israel with bovine mastitis."; RL J. Bacteriol. 193:323-324(2011). RN [2] {ECO:0000313|EMBL:ADL10249.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10249.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21533164; DOI=10.1371/journal.pone.0018551; RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R., RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z., RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L., RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J., RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M., RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T., RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P., RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C., RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.; RT "Evidence for reductive genome evolution and lateral acquisition of RT virulence functions in two Corynebacterium pseudotuberculosis strains."; RL PLoS ONE 6:E18551-E18551(2011). 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 + phosphate + H(+); 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; CP001829; ADL10249.1; -; Genomic_DNA. DR RefSeq; WP_013241623.1; NC_017301.2. DR AlphaFoldDB; D9Q9M3; -. DR STRING; 681645.CpC231_0767; -. DR GeneID; 69460021; -. DR KEGG; cpq:CPC231_03855; -. DR PATRIC; fig|681645.3.peg.797; -. DR eggNOG; COG1217; Bacteria. DR HOGENOM; CLU_017016_4_0_11; -. DR OrthoDB; 9801472at2; -. DR Proteomes; UP000000276; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:TreeGrafter. 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 CDD; cd03710; BipA_TypA_C; 1. DR CDD; cd03691; BipA_TypA_II; 1. DR CDD; cd01891; TypA_BipA; 1. DR FunFam; 2.40.50.250:FF:000001; GTP-binding protein TypA; 1. DR FunFam; 3.30.70.240:FF:000002; GTP-binding protein TypA; 1. DR FunFam; 3.30.70.870:FF:000003; GTP-binding protein TypA; 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; IPR048876; BipA_C. DR InterPro; IPR047041; BipA_GTP-bd_dom. DR InterPro; IPR047042; BipA_II. 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; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. 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; PF21018; BipA_C; 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 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; 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|HAMAP-Rule:MF_00849}; KW Reference proteome {ECO:0000313|Proteomes:UP000000276}; 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 4..221 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 16..21 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" FT BINDING 136..139 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" SQ SEQUENCE 636 AA; 68923 MW; BE5F5FA0F6C232DD CRC64; MTRPEFRNVA IVAHVDHGKT TLVDAMLRQS GAFDEHAELV DRVMDSGDLE KEKGITILAK NTAIRRKGAG KDGNDLVINV IDTPGHADFG GEVERALSMV DGVVLLVDAS EGPLPQTRFV LGKALAAKMP VIILVNKTDR PDARIDEVVE ESQDLLLELA SALDDPEAAE AAEQLLDLPV LYASGREGKA SVENPGNGNI PDAEDLQALF DVIYDVMPEP TVNSEGALQA HVTNLDSSSF LGRIGLIRVH SGTLKKGQQV AWIHYDEDGN QHIKSAKIAE LLRTVGVTRV PADEVVAGDI AAISGIDSVM IGDTLADPEN PVALPRITVD EPAISMTIGV NTSPLAGRGG GDKLTARVVK ARLDQELIGN VSIRVLPTER PDAWEVQGRG EMSLSVLVET MRREGFELTV GKPQVVTQTI DGKLYEPYEH MVIDIPSEYQ GNVTQLMAAR KGQMLSMDNI SDDWVRMEYK VPARGLISFR TIFLTETRGT GIANSYSEGI DEWAGEIKGR ASGSLVADRS GQITAYALTQ LSDRGNFFVE PGMEAYEGMV VGANNRDEDM DVNITKEKKL TNMRSATADA TVTLAKAHVL SLDEAMEFCG QDECVEVTPN ALRVRKVILN ATERGRARAR EKARNK //