GenomeNet

Database: UniProt
Entry: J2G9Y3_9BACL
LinkDB: J2G9Y3_9BACL
Original site: J2G9Y3_9BACL 
ID   J2G9Y3_9BACL            Unreviewed;       613 AA.
AC   J2G9Y3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=PMI05_03202 {ECO:0000313|EMBL:EJL26560.1};
OS   Brevibacillus sp. BC25.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1144308 {ECO:0000313|EMBL:EJL26560.1, ECO:0000313|Proteomes:UP000007278};
RN   [1] {ECO:0000313|EMBL:EJL26560.1, ECO:0000313|Proteomes:UP000007278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC25 {ECO:0000313|EMBL:EJL26560.1,
RC   ECO:0000313|Proteomes:UP000007278};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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:EJL26560.1}.
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; AKIX01000052; EJL26560.1; -; Genomic_DNA.
DR   RefSeq; WP_007723249.1; NZ_AKIX01000052.1.
DR   AlphaFoldDB; J2G9Y3; -.
DR   PATRIC; fig|1144308.3.peg.3166; -.
DR   Proteomes; UP000007278; 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: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; IPR041095; EFG_II.
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; PF14492; EFG_III; 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|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   613 AA;  68875 MW;  43B05FD16145ED2C CRC64;
     MKRLDIRNIA IIAHVDHGKT TLVDKLLIQS GTFRSNQQVE ERMMDSNDLE RERGITILAK
     TTSVKYNDFT INILDTPGHA DFGGEVERIM SMVDGVLLIV DAFEGCMPQT RFVLKKALEA
     KVTPIVVVNK VDRDNARPQE VINEVYDLFI DLDATEDQLE FPIVYASGLQ GIAGLEPDKL
     EGDLRPLFDT IVEHMPAPDA DESAPLQMQV TMLDYNDFLG RIGIGRIYRG TMNLNEMVSV
     TTREGEVKKA RIQKLFGFSG LQRVEQKTAR AGDIVAISGI DDINVGETVC HVDHPEALPL
     LKIDEPTLQM TFLVNNSPFA GREGKHVTSR KLRDRLMSEL ETDVSLRVDE TDSPDAYVVS
     GRGELHLSIL VENMRREGFE LGVSKPEVII RMVDGQKMEP AELLIIDVPE EYTGPVMETL
     GQRKAEMVNM INNGFGQVRL EFIIPSRGLI GYRTEFLTIT RGYGILNHSF DSYRPLVPGA
     VGGRHAGVLI SHETGTATTY GLMSVEDRGT MFIQPGTEVY EGMIVGEHNR DNDLTVNVCK
     EKHATNVRSA TKDETVKMKT PRMLSLEEAL EYLNDDELCE VTPQSVRLRK KYLNKSDRER
     YEKQRRYEAQ PQA
//
DBGET integrated database retrieval system