ID A0A3L9Y515_9RHOB Unreviewed; 606 AA.
AC A0A3L9Y515;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:RMA42137.1};
GN Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN ORFNames=D9R08_11855 {ECO:0000313|EMBL:RMA42137.1};
OS Rhodophyticola porphyridii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodophyticola.
OX NCBI_TaxID=1852017 {ECO:0000313|EMBL:RMA42137.1, ECO:0000313|Proteomes:UP000281343};
RN [1] {ECO:0000313|EMBL:RMA42137.1, ECO:0000313|Proteomes:UP000281343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MA-7-27 {ECO:0000313|EMBL:RMA42137.1,
RC ECO:0000313|Proteomes:UP000281343};
RA Jung H.S., Jeon C.O.;
RL Submitted (OCT-2018) 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:RMA42137.1}.
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DR EMBL; RCNT01000005; RMA42137.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L9Y515; -.
DR OrthoDB; 9802948at2; -.
DR Proteomes; UP000281343; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 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; IPR048876; BipA_C.
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; 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 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|HAMAP-Rule:MF_00849};
KW Reference proteome {ECO:0000313|Proteomes:UP000281343};
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 1..196
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 13..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
FT BINDING 126..129
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
SQ SEQUENCE 606 AA; 66007 MW; D4FA26AB65BC0F40 CRC64;
MDLRNIAIIA HVDHGKTTLV DELLKQSGAF RDNQAVAERA MDSNDLERER GITILAKATS
LEWKGMRINI VDTPGHADFG GEVERILSMV DGVVLLVDAA EGPMPQTKFV TSKALALGLR
PIVVLNKVDK PDAEPDRALD ECFDLFANLG ADDDQLDFPH LYASGRAGWA DDTLDGPRKD
LTALFDLVVS HVPAPKQIAH DKEPFRMLAT TLGSDPFIGR ILTGRVESGT LKAGETVKAL
SRDGEKIEQF RATKILAFRG LGQQPIDIAE AGDIVSIAGM SKATVADTVC DLSVTEAIPA
QPIDPPTITV TFGINDSPLA GKDGKKVQSR VIRERLMKEA ESNVAIRVTD TPGGEAFEVA
GRGELQMGVL IENMRREGFE LSISRPQVLF VEENGEKLEP VEEVTIDVDD EYTGAVIEKL
TGPRKGELSE MKPAGAGKTR IVALVPSRGL IGYHGEFLTD TRGTGVLNRV FHAWEPYKGP
IPGRRAGVLI SMENGTSVAY ALWNLEERGK MFIGAQEAIY TGMIIGEHSR DNDLEVNPLK
GKKLTNVRAS GTDDAVRLTT PITMSLEQAI AYIDDDELVE VTPNAIRLRK RFLDPHERKR
QARAAS
//