ID G4Q308_ACIIR Unreviewed; 606 AA.
AC G4Q308;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
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 OrderedLocusNames=Acin_1597 {ECO:0000313|EMBL:AEQ22814.1};
OS Acidaminococcus intestini (strain RyC-MR95).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ22814.1, ECO:0000313|Proteomes:UP000007093};
RN [1] {ECO:0000313|EMBL:AEQ22814.1, ECO:0000313|Proteomes:UP000007093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ22814.1,
RC ECO:0000313|Proteomes:UP000007093};
RX PubMed=22123762; DOI=10.1128/JB.06301-11;
RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA Latorre A.;
RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT negative bacterium from the phylum Firmicutes.";
RL J. Bacteriol. 193:7008-7009(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 + 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 ---------------------------------------------------------------------------
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; CP003058; AEQ22814.1; -; Genomic_DNA.
DR RefSeq; WP_009015245.1; NC_016077.1.
DR AlphaFoldDB; G4Q308; -.
DR STRING; 568816.Acin_1597; -.
DR GeneID; 72309779; -.
DR KEGG; ain:Acin_1597; -.
DR PATRIC; fig|568816.4.peg.1550; -.
DR eggNOG; COG1217; Bacteria.
DR HOGENOM; CLU_017016_4_0_9; -.
DR InParanoid; G4Q308; -.
DR Proteomes; UP000007093; Chromosome.
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:0042254; P:ribosome biogenesis; 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; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00849}; Reference proteome {ECO:0000313|Proteomes:UP000007093};
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..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 606 AA; 67769 MW; 06F36A8BC10C1501 CRC64;
MIRNDLRNIA IIAHVDHGKT TLVDAMLKQS HVFRANEKVQ ERVMDSNDQE RERGITILAK
NTSVMHEGTK INILDTPGHA DFGGEVERVL NMVDGVLLLV DAYEGPMPQT KYVLRKALEH
HLKPVVVINK IDRPDQRVDE VVDEVLDLFI ELNASDDQLD FPVVYCSAKK GIAKLSMDDD
SDNLDPLFKV IMDTIPAPDV DVDGPLQMLA NTLDYDDYVG RIVVGRIVRG TIKNGQMICL
MHDDQRTNEK IGRLYTYEGL KRVETQEAKA GEIIALIGLQ DVEIGDTIAD SENPEQLAGI
KVDEPTLSMT FSVNDSPFAG QEGDFITSRH IRERLYKEVE TNVSMRVEDT DSPDTFKVSG
RGELHLSVLI EAMRREGFEL QVGKPSVIMR RDENGKLLEP MEALTIDVPQ DFMGPVMEGL
GIRKAELQNM TEMSGYLRME FIIPARGLIG FRSQFLTDTK GNGIMNHVFA GWGAYKGDIP
GRTRGSLVAF EAGETTAYGI DKCQARGTMY INPGEQVYEG QIVGENSRED DMDVNPCKKK
HVSNMRAAGS DDAVRLIPPQ TFSLEGALEH INEDETVEVT PKSIRMRKKI LSRLERARQR
ARNAKA
//
