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Database: UniProt
Entry: F6EST0_SPHCR
LinkDB: F6EST0_SPHCR
Original site: F6EST0_SPHCR 
ID   F6EST0_SPHCR            Unreviewed;       605 AA.
AC   F6EST0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
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=Sphch_0036 {ECO:0000313|EMBL:AEG47739.1};
OS   Sphingobium chlorophenolicum L-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG47739.1, ECO:0000313|Proteomes:UP000007150};
RN   [1] {ECO:0000313|EMBL:AEG47739.1, ECO:0000313|Proteomes:UP000007150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-1 {ECO:0000313|EMBL:AEG47739.1,
RC   ECO:0000313|Proteomes:UP000007150};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Pagani I., Turner P., Copley S., Woyke T.;
RT   "Complete sequence of chromosome 1 of Sphingobium chlorophenolicum L-1.";
RL   Submitted (MAY-2011) 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; CP002798; AEG47739.1; -; Genomic_DNA.
DR   RefSeq; WP_013846012.1; NC_015593.1.
DR   AlphaFoldDB; F6EST0; -.
DR   STRING; 690566.Sphch_0036; -.
DR   KEGG; sch:Sphch_0036; -.
DR   HOGENOM; CLU_017016_4_0_5; -.
DR   Proteomes; UP000007150; Chromosome 1.
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 {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   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
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          1..196
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         13..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00849"
SQ   SEQUENCE   605 AA;  66344 MW;  FE3C86811FFC8D10 CRC64;
     MSLRNIAIIA HVDHGKTTLV DQLFRQSGTF RDNQRVEERA MDSNDLEKER GITILAKPTS
     VEWNGTRINI VDTPGHADFG GEVERILSMV DGVILLVDSS EGAMPQTKFV TGKALALGLR
     PIVVVNKIDR PDERIQEVLD EVFDLFVTLE ANDEQLDFPV LYASGRNGYA NEDPSLRSGT
     LEPLFQKIVD HVPPPALDVD APFSFLVTLL DRDNFLGRIL TGRVNSGTLK VNQPIHAIDA
     DGNVLETGRA SKILSFRGLD RVPVEEARAG DIISLAGLTV ATVANTIADP SVSTAIKAQP
     IDPPTLSMRF AVNDSPMAGR EGSKVTSRMI RDRLMREAES NVAIKVTESA DKDSFEVAGR
     GELQLGVLIE TMRREGFELG ISRPRVLFGE DEAGNKTEPY ETVVIDVDDE FSGTVVDKMN
     IRKAEMTDMR PSGGGKTRIT FSAPSRGLIG YHGEFLSDTR GTGIMNRLFE KYGPHKGKIE
     GRKNGVLISN GAGEAVAYAL GPLEERGILF VGVGEALYEG MVIGENAKPE DLEVNPMKSK
     ALTNFRASGK DDSIRLTPPK KMTLEQAIAY IDDDEMVEVT PKNIRLRKRY LDPNERKRMS
     RAKAA
//
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