BIPA_ECOLI
ID BIPA_ECOLI Reviewed; 607 AA.
AC P0DTT0; P32132; Q2M8G8; Q6BEY2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=50S ribosomal subunit assembly factor BipA {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000303|PubMed:30305394};
DE EC=3.6.5.- {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000269|PubMed:30305394};
DE AltName: Full=GTP-binding protein BipA/TypA;
DE AltName: Full=Ribosome assembly factor BipA;
DE AltName: Full=Ribosome-dependent GTPase BipA;
DE AltName: Full=Tyrosine phosphorylated protein A;
GN Name=bipA {ECO:0000255|HAMAP-Rule:MF_00849, ECO:0000303|PubMed:9622352};
GN Synonyms=o591 {ECO:0000303|PubMed:8346018}, typA, yihK;
GN OrderedLocusNames=b3871, JW5571;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION TO 592-607.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP NOT PHOSPHORYLATED.
RC STRAIN=K12;
RX PubMed=9642082; DOI=10.1006/jmbi.1998.1836;
RA Freestone P., Trinei M., Clarke S.C., Nystroem T., Norris V.;
RT "Tyrosine phosphorylation in Escherichia coli.";
RL J. Mol. Biol. 279:1045-1051(1998).
RN [7]
RP FUNCTION IN EPEC BACTERIA, AND WEAK PHOSPHORYLATION.
RC STRAIN=K12;
RX PubMed=9622352; DOI=10.1046/j.1365-2958.1998.00793.x;
RA Farris M., Grant A., Richardson T.B., O'Connor C.D.;
RT "BipA: a tyrosine-phosphorylated GTPase that mediates interactions between
RT enteropathogenic Escherichia coli (EPEC) and epithelial cells.";
RL Mol. Microbiol. 28:265-279(1998).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=10781541; DOI=10.1128/jb.182.10.2741-2745.2000;
RA Rowe S., Hodson N., Griffiths G., Roberts I.S.;
RT "Regulation of the Escherichia coli K5 capsule gene cluster: evidence for
RT the roles of H-NS, BipA, and integration host factor in regulation of group
RT 2 capsule gene clusters in pathogenic E. coli.";
RL J. Bacteriol. 182:2741-2745(2000).
RN [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / D10, and K12 / MG1655 / ATCC 47076;
RX PubMed=11683274; DOI=10.1007/s004380100559;
RA Pfennig P.L., Flower A.M.;
RT "BipA is required for growth of Escherichia coli K12 at low temperature.";
RL Mol. Genet. Genomics 266:313-317(2001).
RN [10]
RP SUPPRESSION BY RLUC DELETION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=18820021; DOI=10.1128/jb.00835-08;
RA Krishnan K., Flower A.M.;
RT "Suppression of DeltabipA phenotypes in Escherichia coli by abolishment of
RT pseudouridylation at specific sites on the 23S rRNA.";
RL J. Bacteriol. 190:7675-7683(2008).
RN [11]
RP PROBABLE FUNCTION IN RIBOSOMAL ASSEMBLY, SUPPRESSION BY RLUC DELETION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25777676; DOI=10.1128/jb.00023-15;
RA Choudhury P., Flower A.M.;
RT "Efficient assembly of ribosomes is inhibited by deletion of bipA in
RT Escherichia coli.";
RL J. Bacteriol. 197:1819-1827(2015).
RN [12]
RP SUBCELLULAR LOCATION, INDUCTION BY COLD, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RA Cochrane K.L.;
RT "Elucidating Ribosomes-Genetic Studies of the ATPase Uup and the Ribosomal
RT Protein L1.";
RL Thesis (2015), University of Michigan, United States.
RN [13]
RP FUNCTION AS A CHAPERONE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP INDUCTION BY COLD, NOT PHOSPHORYLATED, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF ASN-128; TYR-164; TYR-472 AND TYR-519.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30305394; DOI=10.1074/jbc.ra118.002295;
RA Choi E., Hwang J.;
RT "The GTPase BipA expressed at low temperature in Escherichia coli assists
RT ribosome assembly and has chaperone-like activity.";
RL J. Biol. Chem. 293:18404-18419(2018).
RN [14] {ECO:0007744|PDB:4ZCI, ECO:0007744|PDB:4ZCK, ECO:0007744|PDB:4ZCL, ECO:0007744|PDB:4ZCM}
RP X-RAY CRYSTALLOGRAPHY (3.31 ANGSTROMS) ALONE AND IN COMPLEX WITH GDP AND
RP GUANOSINE 3',5'-BIS(DIPHOSPHATE), X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF
RP 306-603, FUNCTION, SUBUNIT, DOMAIN, AND NUCLEOTIDE-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=26163516; DOI=10.1074/jbc.m115.659136;
RA Fan H., Hahm J., Diggs S., Perry J.J., Blaha G.;
RT "Structural and Functional Analysis of BipA, a Regulator of Virulence in
RT Enteropathogenic Escherichia coli.";
RL J. Biol. Chem. 290:20856-20864(2015).
RN [15] {ECO:0007744|PDB:5A9V, ECO:0007744|PDB:5A9W, ECO:0007744|PDB:5A9X, ECO:0007744|PDB:5A9Y, ECO:0007744|PDB:5A9Z, ECO:0007744|PDB:5AA0}
RP X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) ALONE AND IN COMPLEX WITH GDP;
RP GUANOSINE 3',5'-BIS(DIPHOSPHATE) AND GUANOSINE
RP 5'-[BETA,GAMMA-METHYLENE]TRIPHOSPHATE, STRUCTURE BY ELECTRON MICROSCOPY
RP (4.70 ANGSTROMS) IN COMPLEX WITH T.THERMOPHILUS 70S RIBOSOME, FUNCTION,
RP SUBUNIT, DOMAIN, AND NUCLEOTIDE-BINDING.
RX PubMed=26283392; DOI=10.1073/pnas.1513216112;
RA Kumar V., Chen Y., Ero R., Ahmed T., Tan J., Li Z., Wong A.S., Bhushan S.,
RA Gao Y.G.;
RT "Structure of BipA in GTP form bound to the ratcheted ribosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:10944-10949(2015).
CC -!- FUNCTION: A 50S ribosomal subunit assembly protein with GTPase and
CC nucleotide-independent chaperone activity, required for 50S subunit
CC assembly at low temperatures, may also play a role in translation
CC (PubMed:30305394). Genetic and deletion evidence suggests this is
CC involved in ribosome assembly at low temperatures; it may also affect
CC translation (Probable) (PubMed:25777676, PubMed:30305394). Involved in
CC incorporation of ribosomal protein L6 into precursor 44S ribosomal
CC particles at low temperatures. Also has chaperone activity which does
CC not require nucleotides (PubMed:30305394). Binds GDP, ppGpp and GDPCP
CC (a nonhydrolyzable GTP analog) with similar affinity; the conformation
CC of the protein does not significantly change upon nucleotide binding
CC (PubMed:26163516, PubMed:26283392). Interacts with ribosomes (Ref.12,
CC PubMed:26283392). Binds the 70S ribosome between the 30S and 50S
CC subunits, in a similar position as ribosome-bound EF-G; it contacts a
CC number of ribosomal proteins, both rRNAs and the A-site tRNA. Ribosome
CC binding alters its conformation (PubMed:26283392). Genetically its
CC function does not overlap LepA, and it acts in a different pathway
CC during ribosome assembly than does RNA helicase DeaD (PubMed:25777676).
CC GTPase that affects interactions between enteropathogenic E.coli (EPEC)
CC and epithelial cells (PubMed:9622352). Probably regulates expression of
CC proteins required for (at least) K5 polysaccharide production
CC (Probable). Deletion mutants of bipA are suppressed by an rluC
CC deletion, which no longer modifies uracils 955, 2504 and 2580 to
CC pseudouridine in 23S rRNA; there are 5 other pseudouridine synthases in
CC E.coli, only rluC suppresses this phenotype. Mutating 23S rRNA so the 3
CC uracils are other nucleotides also suppresses the bipA deletion;
CC pseudouridine-2504 is required for ribosome assembly and translational
CC accuracy (PubMed:18820021, PubMed:25777676).
CC {ECO:0000269|PubMed:18820021, ECO:0000269|PubMed:25777676,
CC ECO:0000269|PubMed:26163516, ECO:0000269|PubMed:26283392,
CC ECO:0000269|PubMed:30305394, ECO:0000269|PubMed:9622352,
CC ECO:0000269|Ref.12, ECO:0000305|PubMed:10781541,
CC ECO:0000305|PubMed:18820021}.
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, ECO:0000269|PubMed:30305394};
CC -!- SUBUNIT: Monomer (PubMed:26163516, PubMed:26283392). Binds between the
CC 30S and 50S ribosomal subunits, in a similar position as ribosome-bound
CC EF-G; it contacts proteins L7/12, L11, S2, 16S and 23S rRNA and the A-
CC site tRNA. Binding to the ribosome alters its conformation
CC (PubMed:26283392). {ECO:0000269|PubMed:26163516,
CC ECO:0000269|PubMed:26283392}.
CC -!- INTERACTION:
CC P0DTT0; P75864: rlmL; NbExp=3; IntAct=EBI-562154, EBI-547718;
CC P0DTT0; P0A898: ybeY; NbExp=2; IntAct=EBI-562154, EBI-560240;
CC P0DTT0; P27862: yigZ; NbExp=2; IntAct=EBI-562154, EBI-561235;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00849,
CC ECO:0000269|PubMed:30305394, ECO:0000269|Ref.12}. Note=Associates with
CC 70S ribosomes and 30S and 50S subunits in the presence of GMPPNP (a
CC nonhydrolyzable GTP analog) at both 20 and 37 degrees Celsius; no
CC change in ribosome association is seen in the presence of ppGpp or when
CC the stringent response is triggered. {ECO:0000269|PubMed:30305394}.
CC -!- INDUCTION: Induced about 2-fold at 18 degrees Celsius (at protein
CC level) (Ref.12). Basally expressed at 37 degrees Celsius, 3.5-fold
CC induced after shift to 20 degrees Celsius, maximal expression is seen
CC at 2 hours (at protein level). No increase in expression when cells are
CC grown at 43 degrees Celsius or when engineered to produce increased
CC levels of the stress second messenger ppGpp. Expression at low
CC temperatures is activated by CRP (PubMed:30305394).
CC {ECO:0000269|PubMed:30305394, ECO:0000269|Ref.12}.
CC -!- DOMAIN: Crystallizes with 2 superdomains; the first comprises domains I
CC (residues 1-202, also called the G domain) and II (203-302, also called
CC the beta barrel domain), while the second is composed of domains III
CC (303-385), V (386-482) and a BipA-specific C-terminal domain (CTD, 483-
CC 607). Domains I-V are homologous to domains in EF-G and LepA; although
CC the domains are similar, their relative arrangement is different
CC (PubMed:26163516, PubMed:26283392). The structure of isolated
CC superdomain 2 is more compact in the presence of Mg(2+) than in the
CC intact protein (PubMed:26163516). Upon ribosome binding the second
CC superdomain shifts and the CTD assumes a more compact conformation. The
CC CTD binds to the A-site tRNA (PubMed:26283392). Chaperone activity
CC resides in domain I; truncated proteins of 49-607 and 149-607 have no
CC chaperone activity (PubMed:30305394). {ECO:0000269|PubMed:26163516,
CC ECO:0000269|PubMed:26283392, ECO:0000269|PubMed:30305394}.
CC -!- PTM: Very poorly to not phosphorylated on tyrosine (PubMed:9622352,
CC PubMed:9642082, PubMed:30305394). Phosphorylation in vitro is strongly
CC activated by proteins present in pathogenic strain E2348/69 / EPEC /
CC MAR001 but not non-pathogenic strain K12 / DH5 alpha. Phosphorylation
CC in vitro increases GTPase activity (PubMed:9622352). Mutation of 3
CC conserved Tyr residues (Tyr-164; Ty5-47 or Tyr-591) to Phe alone or in
CC all combinations has no effect on the ability of the protein to restore
CC growth to a deletion mutant, suggesting Tyr-phosphorylation is not
CC important in non-EPEC strains (PubMed:30305394).
CC {ECO:0000269|PubMed:30305394, ECO:0000269|PubMed:9622352,
CC ECO:0000269|PubMed:9642082}.
CC -!- DISRUPTION PHENOTYPE: Decreased extracellular K5 polysaccharide
CC production at 37 degrees Celsius, increased extracellular K5
CC polysaccharide production at 20 degrees Celsius (PubMed:10781541).
CC Cold-sensitive growth (20 degrees Celsius); cells have a long lag phase
CC and double more slowly (PubMed:11683274, PubMed:18820021). Decreased
CC capsule synthesis. Cold sensitive growth and decreased capsule
CC synthesis are suppressed by an rluC deletion (PubMed:18820021). Cold-
CC sensitive growth (20 degrees Celsius); a single bipA deletion has a
CC disturbed ribosome profile at low temperature, with more 30S than 50S
CC subunits, accumulation of a precursor-23S rRNA and precursor 50S
CC subunit and decreased 70S ribosomes (PubMed:25777676, PubMed:30305394).
CC These ribosome phenotypes are suppressed in an rluC deletion. A double
CC bipA-deaD deletion has a more severe growth and ribosome phenotype than
CC either single deletion (PubMed:25777676). At 20 degrees Celsius the
CC single deletion is missing ribosomal protein L6 and has decreased
CC amounts of L9 and L18 and makes less capsule. It has decreased motility
CC at both 20 and 37 degrees Celsius (PubMed:30305394). Cold-sensitive
CC growth (18 degrees Celsius); 2-fold more Uup is expressed at 37 degrees
CC Celsius, 10-fold more Uup at 18 degrees Celsius. A double bipA-uup
CC deletion does not grow at 18 degrees Celsius (Ref.12).
CC {ECO:0000269|PubMed:10781541, ECO:0000269|PubMed:11683274,
CC ECO:0000269|PubMed:18820021, ECO:0000269|PubMed:25777676,
CC ECO:0000269|PubMed:30305394, ECO:0000269|Ref.12}.
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; L19201; AAB03005.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48232.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77438.1; -; Genomic_DNA.
DR PIR; S40816; S40816.
DR RefSeq; WP_000570668.1; NZ_STEB01000017.1.
DR RefSeq; YP_026274.1; NC_000913.3.
DR PDB; 4ZCI; X-ray; 2.63 A; A/B=1-601.
DR PDB; 4ZCK; X-ray; 2.48 A; A=306-603.
DR PDB; 4ZCL; X-ray; 3.06 A; A/B=1-601.
DR PDB; 4ZCM; X-ray; 3.31 A; A/B=1-607.
DR PDB; 5A9V; X-ray; 3.31 A; A/B/C/D/E/F=1-607.
DR PDB; 5A9W; X-ray; 3.70 A; A=1-607.
DR PDB; 5A9X; X-ray; 3.80 A; A=1-607.
DR PDB; 5A9Y; X-ray; 4.00 A; A=1-607.
DR PDB; 5A9Z; EM; 4.70 A; CA=1-605.
DR PDB; 5AA0; EM; 5.00 A; BZ=1-605.
DR PDBsum; 4ZCI; -.
DR PDBsum; 4ZCK; -.
DR PDBsum; 4ZCL; -.
DR PDBsum; 4ZCM; -.
DR PDBsum; 5A9V; -.
DR PDBsum; 5A9W; -.
DR PDBsum; 5A9X; -.
DR PDBsum; 5A9Y; -.
DR PDBsum; 5A9Z; -.
DR PDBsum; 5AA0; -.
DR AlphaFoldDB; P0DTT0; -.
DR SMR; P0DTT0; -.
DR DIP; DIP-11058N; -.
DR IntAct; P0DTT0; 5.
DR STRING; 511145.b3871; -.
DR jPOST; P0DTT0; -.
DR GeneID; 66672223; -.
DR GeneID; 948369; -.
DR KEGG; ecj:JW5571; -.
DR KEGG; eco:b3871; -.
DR EchoBASE; EB1783; -.
DR OMA; MSMLFTI; -.
DR BRENDA; 3.6.5.3; 2026.
DR PRO; PR:P0DTT0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Hydrolase; Nucleotide-binding; Reference proteome; Ribosome biogenesis;
KW RNA-binding; rRNA-binding; tRNA-binding.
FT CHAIN 1..607
FT /note="50S ribosomal subunit assembly factor BipA"
FT /id="PRO_0000091550"
FT DOMAIN 3..198
FT /note="tr-type G"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849"
FT REGION 1..202
FT /note="Domain I (or G domain), required for chaperone
FT activity"
FT /evidence="ECO:0000269|PubMed:30305394,
FT ECO:0000305|PubMed:26163516, ECO:0000305|PubMed:26283392"
FT REGION 203..320
FT /note="Domain II (or beta barrel domain)"
FT /evidence="ECO:0000305|PubMed:26163516,
FT ECO:0000305|PubMed:26283392"
FT REGION 303..385
FT /note="Domain III"
FT /evidence="ECO:0000305|PubMed:26163516,
FT ECO:0000305|PubMed:26283392"
FT REGION 386..482
FT /note="Domain V"
FT /evidence="ECO:0000305|PubMed:26163516,
FT ECO:0000305|PubMed:26283392"
FT REGION 483..607
FT /note="C-terminal domain (CTD), binds A-site tRNA"
FT /evidence="ECO:0000305|PubMed:26163516,
FT ECO:0000305|PubMed:26283392"
FT BINDING 15..20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849,
FT ECO:0000269|PubMed:26163516, ECO:0000269|PubMed:26283392,
FT ECO:0007744|PDB:4ZCL, ECO:0007744|PDB:4ZCM,
FT ECO:0007744|PDB:5A9W, ECO:0007744|PDB:5A9Y"
FT BINDING 128..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00849,
FT ECO:0000269|PubMed:26163516, ECO:0007744|PDB:4ZCL,
FT ECO:0007744|PDB:4ZCM, ECO:0007744|PDB:5A9Y"
FT BINDING 166..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:26163516,
FT ECO:0007744|PDB:4ZCL, ECO:0007744|PDB:4ZCM,
FT ECO:0007744|PDB:5A9W"
FT MUTAGEN 128
FT /note="N->D: No GTPase activity, does not restore normal
FT ribosomes to a bipA deletion, does not associate with
FT ribosomes, retains its ability to help proteins refold."
FT /evidence="ECO:0000269|PubMed:30305394"
FT MUTAGEN 164
FT /note="Y->P: No change in growth at 20 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:30305394"
FT MUTAGEN 472
FT /note="Y->P: No change in growth at 20 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:30305394"
FT MUTAGEN 519
FT /note="Y->P: No change in growth at 20 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:30305394"
FT CONFLICT 592..607
FT /note="Missing (in Ref. 1; AAB03005)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:4ZCI"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:4ZCM"
FT HELIX 84..89
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:4ZCI"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4ZCI"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4ZCI"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4ZCI"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:4ZCI"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:4ZCL"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4ZCI"
FT TURN 167..170
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:4ZCI"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4ZCI"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:4ZCI"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:4ZCK"
FT TURN 317..320
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:4ZCK"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 363..375
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 395..408
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 409..421
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 435..444
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 464..474
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 498..504
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 522..531
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 533..535
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 542..546
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:4ZCK"
FT STRAND 584..591
FT /evidence="ECO:0007829|PDB:4ZCK"
FT HELIX 594..601
FT /evidence="ECO:0007829|PDB:4ZCK"
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
