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Database: UniProt
Entry: A0A387BNI6_9MICO
LinkDB: A0A387BNI6_9MICO
Original site: A0A387BNI6_9MICO 
ID   A0A387BNI6_9MICO        Unreviewed;       639 AA.
AC   A0A387BNI6;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:AYG02557.1};
GN   Synonyms=bipA {ECO:0000256|HAMAP-Rule:MF_00849};
GN   ORFNames=D7I44_02795 {ECO:0000313|EMBL:AYG02557.1};
OS   Gryllotalpicola protaetiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Gryllotalpicola.
OX   NCBI_TaxID=2419771 {ECO:0000313|EMBL:AYG02557.1, ECO:0000313|Proteomes:UP000275069};
RN   [1] {ECO:0000313|EMBL:AYG02557.1, ECO:0000313|Proteomes:UP000275069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2DFW10M-5 {ECO:0000313|EMBL:AYG02557.1,
RC   ECO:0000313|Proteomes:UP000275069};
RA   Heo J., Kim S.-J., Kwon S.-W.;
RT   "Genome sequencing of strain 2DFW10M-5.";
RL   Submitted (SEP-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}.
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DR   EMBL; CP032624; AYG02557.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A387BNI6; -.
DR   KEGG; gry:D7I44_02795; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000275069; 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; 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; 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:UP000275069};
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          7..228
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         19..24
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
FT   BINDING         143..146
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
SQ   SEQUENCE   639 AA;  69471 MW;  353298E7E55FA9C5 CRC64;
     MATALRTDLR NVAIVAHVDH GKTTLVDAML KQTNSFGEHA HVEERAMDSN ELEREKGITI
     LAKNTAISYN GEHAAAHNPG GPITINVIDT PGHADFGGEV ERGLSMVDGV VLLVDASEGP
     LPQTRFVLRK ALEAKLPVIL AVNKTDRPDA RIDEVVAEAQ DLLLGLASDL SDDVPDLDVD
     ALLDVPVVYA SGKAGRASRN QPADGSLPDS ENLEPLFEAI LAHIPAPTYD DDAPLQAWVT
     NLDASPFLGR LALLRIFSGT IKKGQTVTRV HHDGTTSNAR ITELLITKAL DRFPAESGSA
     GDIVAVAGIE DIMIGETLAD PDDVRPLPAI HVDEPAISMT VGINTSPLMG KVKGHKLTAR
     MVKDRLDREL VGNVSIRVLD IGKPDAWEVQ GRGELALAIL VEQMRREGFE LTVGKPQVVT
     RKVDGKVHEP YEHVTIDIPE EYLGAITQLL AARKGRMEGM SNHGTGWVRM EFIVPSRGLI
     GFRTEFLTTT RGTGISNAIS HGYDEWAGSI VTRNNGSIVA DRQGVVTAYA IIGLQERMSF
     FVNPTEEVYE GMVVGENSRA DDMDVNITRE KKLTNMRTST ADNFEAMTPS RQLTLEECLE
     FAREDECVEV TPEKVRIRKV ELDATARGRA AARLKKQDA
//
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