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Database: UniProt
Entry: Q89AC9
LinkDB: Q89AC9
Original site: Q89AC9 
ID   BIPA_BUCBP              Reviewed;         611 AA.
AC   Q89AC9;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Large ribosomal subunit assembly factor BipA {ECO:0000255|HAMAP-Rule:MF_00849};
DE            EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_00849};
DE   AltName: Full=50S ribosomal subunit assembly factor BipA {ECO:0000305};
DE   AltName: Full=GTP-binding protein BipA {ECO:0000255|HAMAP-Rule:MF_00849};
GN   Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849}; OrderedLocusNames=bbp_384;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00849};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00849}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849}.
CC       Note=Binds to ribosomes. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00849}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO27096.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE016826; AAO27096.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044010641.1; NC_004545.1.
DR   AlphaFoldDB; Q89AC9; -.
DR   SMR; Q89AC9; -.
DR   STRING; 224915.bbp_384; -.
DR   KEGG; bab:bbp_384; -.
DR   eggNOG; COG1217; Bacteria.
DR   HOGENOM; CLU_017016_4_0_6; -.
DR   OrthoDB; 9804431at2; -.
DR   Proteomes; UP000000601; 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: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: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   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; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; tRNA-binding.
FT   CHAIN           1..611
FT                   /note="Large ribosomal subunit assembly factor BipA"
FT                   /id="PRO_0000091549"
FT   DOMAIN          7..202
FT                   /note="tr-type G"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT   BINDING         19..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT   BINDING         132..135
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
SQ   SEQUENCE   611 AA;  69146 MW;  6D238E8AAE1D7B09 CRC64;
     MQKKTNKNLR NIAIIAHVDH GKTTLVDKLL QQSGTFKKHE EFSERIMDSN DLEKERGITI
     LAKNTAIQWK KYRINIIDTP GHADFGGEVE RILSMVDSVL LVVDALEGPM PQTRFVTQKA
     FSYGIKPIVV INKIDRKHAR PNWVIDQIFD LFVNLNATDE QLDFPTIYTS ALLGTSGVSY
     NHMNPDMIPL YNAIVKYTPP PTVYPNCPFQ MQISQLDYDN YLGIIGIGRI NKGSVTSNQS
     ISIINNTEVK RTGKIGKILQ YLGLNKIEIN EAQSGDIIAI TGIDKLNISD TICDPQYISA
     LPMLKIDEPT VEMLFSVNKS PFSGTEGKYI TSRQIFNRLK KEENYNVALK IKETNDTNTF
     SVSGRGELHL SILIENMRRE GFELEVSRPQ VILKTINELI QEPMETVVLD IENKYQGTIM
     KTIGQRKGTI SNITPDQNNE RTRLDCIISS RSLIGFRTEF STLTSGSGLF YSTFSHYQKI
     ESNKIKRHRN GVLIANKTGQ AIGFSLFNLQ NRGKLFITHG TKVYEGQIVG IHNRVNDLTV
     NCLSGKKLTN MRASGSDEAI TLTTPIKMTL EYAISFINDD ELVEITPKSI RLRKRYLKEN
     ERKILLRNIK E
//
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