ID A0AA91Z3S5_WOLPI Unreviewed; 609 AA. AC A0AA91Z3S5; DT 27-MAR-2024, integrated into UniProtKB/TrEMBL. DT 27-MAR-2024, sequence version 1. DT 29-MAY-2024, entry version 2. 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=bipA {ECO:0000256|HAMAP-Rule:MF_00849}; GN ORFNames=BTO27_02095 {ECO:0000313|EMBL:PBQ28195.1}; OS Wolbachia pipientis wAus. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Anaplasmataceae; Wolbachieae; Wolbachia. OX NCBI_TaxID=2049495 {ECO:0000313|EMBL:PBQ28195.1, ECO:0000313|Proteomes:UP000218032}; RN [1] {ECO:0000313|EMBL:PBQ28195.1, ECO:0000313|Proteomes:UP000218032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=wAus {ECO:0000313|Proteomes:UP000218032}; RA Ward C.M., Baxter S.W.; RT "Wolbachia endosymbiont of Plutella Australiana."; RL Submitted (DEC-2016) 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:PBQ28195.1}. 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; MRWX01000013; PBQ28195.1; -; Genomic_DNA. DR RefSeq; WP_007302691.1; NZ_MRWX01000013.1. DR Proteomes; UP000218032; Unassembled WGS sequence. 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; 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; 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; 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; 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|HAMAP-Rule:MF_00849}; KW 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 5..200 FT /note="Tr-type G" FT /evidence="ECO:0000259|PROSITE:PS51722" FT BINDING 17..22 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" FT BINDING 130..133 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849" SQ SEQUENCE 609 AA; 67256 MW; 2B2FD7BD20496F9E CRC64; MSEFKSIRNI AIIAHVDHGK TTLLDNMLKQ SGTFRENQEV QERVMDSGDQ ERERGITILA KCTSIMWGDE KINIIDTPGH ADFGGEVERV LCMADGVLLL VDAAEGPMPQ TKFVLSKALK ANLKPIVIIN KVDRPDSRID EVLNEIYELF FNLDATNEQL DFPVLYASGR NGWCAKELSD ERKDLSPLFS TVIDYIKPSV YDQNAPFAML VTLLESDKFL GRILTGKIYQ GIAQVNSDLK VIDLDGQVVE RGRLTKLLSF SGLKRVPVEQ AVAGDIIAIA GLEKASVSDT IAAPEVTTAI SSTPVDPPTM AITISVNDSP FAGQEGTKLT STVIKDRLYA EAETNVAITV TLAPSGEAFE VGGRGELQLG VLIENMRREG FELSVSRPRV LFKEEDGKKL EPIEEVVIDV DDEYSGIIME KLSFRKGEVT DMRPSGSGRT RLTFLVPSRG LIGYQGEFLT DSRGTGIINR LFHSYAPHKG SISGRRNGVL ISTDKGEAVA YAIFNLQDRG IMFVKPQDKV YCGMIVGQHS RDNDLEINVL KGKQLTNVRA SGSDEAIKLT PPKIMTLEDM IAYIDDDELV EVTPKSIRLR KKFLDPNERK RAGRAKNKE //