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Database: UniProt
Entry: A0A075R7K5_BRELA
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ID   A0A075R7K5_BRELA        Unreviewed;       608 AA.
AC   A0A075R7K5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:AIG27849.1};
GN   Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN   ORFNames=BRLA_c035370 {ECO:0000313|EMBL:AIG27849.1};
OS   Brevibacillus laterosporus LMG 15441.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1042163 {ECO:0000313|EMBL:AIG27849.1, ECO:0000313|Proteomes:UP000005850};
RN   [1] {ECO:0000313|EMBL:AIG27849.1, ECO:0000313|Proteomes:UP000005850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 15441 {ECO:0000313|EMBL:AIG27849.1,
RC   ECO:0000313|Proteomes:UP000005850};
RX   PubMed=21914864; DOI=10.1128/JB.05696-11;
RA   Djukic M., Poehlein A., Thurmer A., Daniel R.;
RT   "Genome sequence of Brevibacillus laterosporus LMG 15441, a pathogen of
RT   invertebrates.";
RL   J. Bacteriol. 193:5535-5536(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}.
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DR   EMBL; CP007806; AIG27849.1; -; Genomic_DNA.
DR   RefSeq; WP_003336636.1; NZ_CP007806.1.
DR   AlphaFoldDB; A0A075R7K5; -.
DR   STRING; 1042163.BRLA_c035370; -.
DR   KEGG; blr:BRLA_c035370; -.
DR   eggNOG; COG1217; Bacteria.
DR   HOGENOM; CLU_017016_4_0_9; -.
DR   Proteomes; UP000005850; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005850};
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   608 AA;  68197 MW;  7E84FB117BA4F7E9 CRC64;
     MKRLDIRNIA IIAHVDHGKT TLVDKLLIQS GTFRSNQHVA ERMMDSNDLE RERGITILAK
     TTSVKYMDYT INILDTPGHA DFGGEVERIM SMVDGVLLIV DAFEGCMPQT RFVLRKALEA
     NVTPIVVVNK IDRDNARPQE VINEVYDLFI DLDATEEQLD FPIVYASGIK GIAGKEPDSL
     SEDLKPLFDT IIEGIPAPEA NEEEPLQFQV TMLDYNDFLG RIGIGRVYRG VINLNDQVSV
     VKRDGSIKKM RVQKLFGFQG LNRVEQKTAR AGDIIAVAGL EDINVGETVC NADKPDPLPL
     LKIDEPTLQM TFLVNNSPFA GKEGKHVTSR KLRDRLMAEL ETDVSLRVEE SDSADAFIVS
     GRGELHLSIL VENMRREGYE LGVSKPEVII REIDGVKMEP TERLIIDVPE EHTGPVMETL
     GARKAEMVNM INNGFGQVRL EFLIPSRGLI GYRTEFMTIT RGYGILNHSF DSYRPVVPGI
     VGGRRAGVLI SNDTGTASTY GLMSVEDRGV MFIHPGTDVY EGMIVGEHSR DNDLTVNVIK
     EKHATNVRSA NKDETVKMKT PRILSLEEAL EYLNDDELCE VTPQSVRLRK KYLNKSDRER
     YNKTRRFD
//
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