ID A0A7C7F229_XANVA Unreviewed; 609 AA. AC A0A7C7F229; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 03-AUG-2022, entry version 6. 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:HHZ52503.1}; GN Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849}; GN ORFNames=HH294_19615 {ECO:0000313|EMBL:HHZ52503.1}; OS Xanthomonas vasicola pv. zeae. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=2164062 {ECO:0000313|EMBL:HHZ52503.1, ECO:0000313|Proteomes:UP000543001}; RN [1] {ECO:0000313|EMBL:HHZ52503.1, ECO:0000313|Proteomes:UP000543001} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=X23 {ECO:0000313|EMBL:HHZ52503.1, RC ECO:0000313|Proteomes:UP000543001}; RX PubMed=32040377; RA Perez-Quintero A.L., Ortiz-Castro M., Lang J.M., Rieux A., Wu G., Liu S., RA Chapman T.A., Chang C., Ziegle J., Peng Z., White F.F., Plazas M.C., RA Leach J.E., Broders K.; RT "Genomic Acquisitions in Emerging Populations of Xanthomonas vasicola pv. RT vasculorum Infecting Corn in the United States and Argentina."; RL Phytopathology PHYTO03190077R:PHYTO03190077R-PHYTO031900770(2020). 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:HHZ52503.1}. 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; DUWP01000056; HHZ52503.1; -; Genomic_DNA. DR RefSeq; WP_047698126.1; NZ_QCXJ01000004.1. DR GeneID; 64095489; -. DR Proteomes; UP000543001; 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 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}; 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..199 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 129..132 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" SQ SEQUENCE 609 AA; 67266 MW; 47B1EE4A146F7A56 CRC64; MSIEKLRNIA IVAHVDHGKT TLVDCLLKQS GTLSERTVLA ERVMDSNDQE KERGITILAK NTAITWNGNR INIVDTPGHA DFGGEVERVL SMVDSVLILV DAMDGPMPQT RFVTQKAFAM GFKPIVVVNK IDRPGARPDW VIDQVFDLFD KLGATDEQLD FPIVYTSALN GYASLDSDVR DGDMTPLYEA IMQHVSAPDV DPDGPFQMRI SQLDYNNFVG VIGIGRIQRG VLKKNMPVSV IDREGKKRQG KVLQVLGFLG LERIEQDTAE AGDIVAISGV TELTISDTVC ALDHPESLPA LTVDEPTISM TFQVNNSPFA GNKDLSGGKF LTSRQLRDRL DREKVHNVAL KVEEGSDADK FLVSGRGELH LSVLIENMRR EGYELAVSRP EVIIKEIDGK LMEPIEQLVV DIEEQHQGGV MEKLGTRKGQ LKNMEPDGKG RVRLDYMIPA RGLIGFQNEF RTLTQGSGLL FHVFDHYGPK EQGAIAKRQN GVMIANAPGA TPAYALGPLE ERGRLFAAEG DNVYEGQLIG IHSKDNDLTV NAIKTKPLTN MRASGKDDAI KLTPAIKYTL EQALDFIEDD ELVEVTPKEI RLRKKFLTES DRKRAGRSG //