BIPA_ECOL6
ID BIPA_ECOL6 Reviewed; 607 AA.
AC P0A3B1; Q9EXN7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=50S 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=GTP-binding protein BipA {ECO:0000255|HAMAP-Rule:MF_00849};
GN Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000303|PubMed:30597160};
GN Synonyms=typA; OrderedLocusNames=c4820;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=30597160; DOI=10.1016/j.jmb.2018.12.013;
RA Murina V., Kasari M., Takada H., Hinnu M., Saha C.K., Grimshaw J.W.,
RA Seki T., Reith M., Putrins M., Tenson T., Strahl H., Hauryliuk V.,
RA Atkinson G.C.;
RT "ABCF ATPases involved in protein synthesis, ribosome assembly and
RT antibiotic resistance: structural and functional diversification across the
RT tree of life.";
RL J. Mol. Biol. 431:3568-3590(2019).
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 -!- DISRUPTION PHENOTYPE: Wild-type growth at 37 degrees Celsius, at 18
CC degrees grows much more slowly, reaches stationary phase at a lower
CC cell density, seriously decreased amounts of 70S ribosomes. A double
CC bipA-uup deletion has a more severe growth phenotype, low 70S ribosomes
CC but higher amounts of 50S ribosomal subunits than the single bipA
CC deletion. The growth phenotype is suppressed by low ectopic expression
CC of Uup. {ECO:0000269|PubMed:30597160}.
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}.
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DR EMBL; AE014075; AAN83249.1; -; Genomic_DNA.
DR RefSeq; WP_000570668.1; NC_004431.1.
DR AlphaFoldDB; P0A3B1; -.
DR SMR; P0A3B1; -.
DR STRING; 199310.c4820; -.
DR EnsemblBacteria; AAN83249; AAN83249; c4820.
DR GeneID; 66672223; -.
DR KEGG; ecc:c4820; -.
DR eggNOG; COG1217; Bacteria.
DR HOGENOM; CLU_017016_4_0_6; -.
DR OMA; MSMLFTI; -.
DR BioCyc; ECOL199310:C4820-MON; -.
DR Proteomes; UP000001410; 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:0000027; P:ribosomal large subunit assembly; IEA:UniProtKB-UniRule.
DR CDD; cd03710; BipA_TypA_C; 1.
DR Gene3D; 2.40.50.250; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00849; BipA; 1.
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 InterPro; IPR006298; TypA_GTP-bd.
DR PANTHER; PTHR42908:SF8; PTHR42908:SF8; 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR TIGRFAMs; TIGR01394; TypA_BipA; 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; Ribosome biogenesis;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..607
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000091552"
FT DOMAIN 3..198
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
SQ SEQUENCE 607 AA; 67355 MW; 3B4DE3A514F95FFB CRC64;
MIEKLRNIAI IAHVDHGKTT LVDKLLQQSG TFDSRAETQE RVMDSNDLEK ERGITILAKN
TAIKWNDYRI NIVDTPGHAD FGGEVERVMS MVDSVLLVVD AFDGPMPQTR FVTKKAFAYG
LKPIVVINKV DRPGARPDWV VDQVFDLFVN LDATDEQLDF PIVYASALNG IAGLDHEDMA
EDMTPLYQAI VDHVPAPDVD LDGPFQMQIS QLDYNSYVGV IGIGRIKRGK VKPNQQVTII
DSEGKTRNAK VGKVLGHLGL ERIETDLAEA GDIVAITGLG ELNISDTVCD TQNVEALPAL
SVDEPTVSMF FCVNTSPFCG KEGKFVTSRQ ILDRLNKELV HNVALRVEET EDADAFRVSG
RGELHLSVLI ENMRREGFEL AVSRPKVIFR EIDGRKQEPY ENVTLDVEEQ HQGSVMQALG
ERKGDLKNMN PDGKGRVRLD YVIPSRGLIG FRSEFMTMTS GTGLLYSTFS HYDDVRPGEV
GQRQNGVLIS NGQGKAVAFA LFGLQDRGKL FLGHGAEVYE GQIIGIHSRS NDLTVNCLTG
KKLTNMRASG TDEAVVLVPP IRMTLEQALE FIDDDELVEV TPTSIRIRKR HLTENDRRRA
NRAPKDD
