RBBA_ECOLI
ID RBBA_ECOLI Reviewed; 911 AA.
AC P37624; P37625; Q2M7E9; Q6BF27;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Ribosome-associated ATPase {ECO:0000305};
DE AltName: Full=Ribosomal bound ATPase {ECO:0000303|PubMed:10607404};
GN Name=rbbA {ECO:0000303|PubMed:10607404}; Synonyms=yhiG, yhiH;
GN OrderedLocusNames=b3486, JW5676;
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=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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.
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 FUNCTION, ATPASE ACTIVITY, AND INTERACTION WITH RIBOSOMES.
RX PubMed=10607404; DOI=10.1016/s0300-9084(99)00352-1;
RA Kiel M.C., Aoki H., Ganoza M.C.;
RT "Identification of a ribosomal ATPase in Escherichia coli cells.";
RL Biochimie 81:1097-1108(1999).
RN [6]
RP ACTIVITY REGULATION.
RX PubMed=11557474; DOI=10.1128/aac.45.10.2813-2819.2001;
RA Ganoza M.C., Kiel M.C.;
RT "A ribosomal ATPase is a target for hygromycin B inhibition on Escherichia
RT coli ribosomes.";
RL Antimicrob. Agents Chemother. 45:2813-2819(2001).
RN [7]
RP FUNCTION, ATPASE ACTIVITY, ACTIVITY REGULATION, AND INTERACTION WITH
RP RIBOSOMES; EF-TU AND 16S RRNA.
RX PubMed=11168361; DOI=10.1046/j.1432-1033.2001.01873.x;
RA Kiel M.C., Ganoza M.C.;
RT "Functional interactions of an Escherichia coli ribosomal ATPase.";
RL Eur. J. Biochem. 268:278-286(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH RIBOSOMES.
RX PubMed=16495476; DOI=10.1093/nar/gkj508;
RA Xu J., Kiel M.C., Golshani A., Chosay J.G., Aoki H., Ganoza M.C.;
RT "Molecular localization of a ribosome-dependent ATPase on Escherichia coli
RT ribosomes.";
RL Nucleic Acids Res. 34:1158-1165(2006).
RN [9]
RP INTERACTION WITH YHJD, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=21556145; DOI=10.1371/journal.pone.0018510;
RA Babu M., Aoki H., Chowdhury W.Q., Gagarinova A., Graham C., Phanse S.,
RA Laliberte B., Sunba N., Jessulat M., Golshani A., Emili A.,
RA Greenblatt J.F., Ganoza M.C.;
RT "Ribosome-dependent ATPase interacts with conserved membrane protein in
RT Escherichia coli to modulate protein synthesis and oxidative
RT phosphorylation.";
RL PLoS ONE 6:E18510-E18510(2011).
CC -!- FUNCTION: Exhibits an intrinsic ATPase activity that is stimulated by
CC both 70S ribosomes and 30S ribosomal subunits. Could be involved in
CC protein-chain elongation and in release of deacyl-tRNA from ribosomes
CC after peptide bond synthesis. Stimulates the synthesis of
CC polyphenylalanine in vitro. {ECO:0000269|PubMed:10607404,
CC ECO:0000269|PubMed:11168361, ECO:0000269|PubMed:16495476}.
CC -!- ACTIVITY REGULATION: Hygromycin B inhibits RbbA ATPase activity and
CC releases RbbA from 70S ribosomes. {ECO:0000269|PubMed:11168361,
CC ECO:0000269|PubMed:11557474}.
CC -!- SUBUNIT: Interacts with both 70S ribosomes and 30S ribosomal subunits,
CC and with 16S RNA (PubMed:10607404, PubMed:11168361, PubMed:16495476).
CC Binds EF-Tu (PubMed:11168361). Co-purifies with the inner membrane
CC protein YhjD (PubMed:21556145). {ECO:0000269|PubMed:10607404,
CC ECO:0000269|PubMed:11168361, ECO:0000269|PubMed:16495476,
CC ECO:0000269|PubMed:21556145}.
CC -!- INTERACTION:
CC P37624; P76015: dhaK; NbExp=2; IntAct=EBI-544500, EBI-544485;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:21556145}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is slightly elongated at both 15
CC and 32 degrees Celsius and displays a significant loss of translation
CC fidelity. {ECO:0000269|PubMed:21556145}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ABC-2 integral
CC membrane protein family. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18462.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00039; AAB18461.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00039; AAB18462.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U00096; AAT48187.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77807.1; -; Genomic_DNA.
DR PIR; A65146; A65146.
DR RefSeq; WP_000149156.1; NZ_SSZK01000042.1.
DR RefSeq; YP_026225.1; NC_000913.3.
DR AlphaFoldDB; P37624; -.
DR SMR; P37624; -.
DR BioGRID; 4259649; 268.
DR DIP; DIP-12363N; -.
DR IntAct; P37624; 1.
DR STRING; 511145.b3486; -.
DR jPOST; P37624; -.
DR PaxDb; P37624; -.
DR PRIDE; P37624; -.
DR EnsemblBacteria; AAT48187; AAT48187; b3486.
DR EnsemblBacteria; BAE77807; BAE77807; BAE77807.
DR GeneID; 947998; -.
DR KEGG; ecj:JW5676; -.
DR KEGG; eco:b3486; -.
DR PATRIC; fig|1411691.4.peg.3238; -.
DR EchoBASE; EB2136; -.
DR eggNOG; COG0842; Bacteria.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_16_3_6; -.
DR InParanoid; P37624; -.
DR OMA; FTENFTD; -.
DR PhylomeDB; P37624; -.
DR BioCyc; EcoCyc:YHIH-MON; -.
DR PRO; PR:P37624; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0060187; C:cell pole; IDA:EcoCyc.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
DR GO; GO:0045727; P:positive regulation of translation; IDA:EcoCyc.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000412; ABC_2_transport.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51012; ABC_TM2; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..911
FT /note="Ribosome-associated ATPase"
FT /id="PRO_0000093190"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 796..816
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 886..906
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 13..248
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 277..507
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 683..909
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
FT BINDING 45..52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 309..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 911 AA; 100785 MW; 683E1EBB62E6B69E CRC64;
MTHLELVPVP PVAQLAGVSQ HYGKTVALNN ITLDIPARCM VGLIGPDGVG KSSLLSLISG
ARVIEQGNVM VLGGDMRDPK HRRDVCPRIA WMPQGLGKNL YHTLSVYENV DFFARLFGHD
KAEREVRINE LLTSTGLAPF RDRPAGKLSG GMKQKLGLCC ALIHDPELLI LDEPTTGVDP
LSRSQFWDLI DSIRQRQSNM SVLVATAYME EAERFDWLVA MNAGEVLATG SAEELRQQTQ
SATLEEAFIN LLPQAQRQAH QAVVIPPYQP ENAEIAIEAR DLTMRFGSFV AVDHVNFRIP
RGEIFGFLGS NGCGKSTTMK MLTGLLPASE GEAWLFGQPV DPKDIDTRRR VGYMSQAFSL
YNELTVRQNL ELHARLFHIP EAEIPARVAE MSERFKLNDV EDILPESLPL GIRQRLSLAV
AVIHRPEMLI LDEPTSGVDP VARDMFWQLM VDLSRQDKVT IFISTHFMNE AERCDRISLM
HAGKVLASGT PQELVEKRGA ASLEEAFIAY LQEAAGQSNE AEAPPVVHDT THAPRQGFSL
RRLFSYSRRE ALELRRDPVR STLALMGTVI LMLIMGYGIS MDVENLRFAV LDRDQTVSSQ
AWTLNLSGSR YFIEQPPLTS YDELDRRMRA GDITVAIEIP PNFGRDIARG TPVELGVWID
GAMPSRAETV KGYVQAMHQS WLQDVASRQS TPASQSGLMN IETRYRYNPD VKSLPAIVPA
VIPLLLMMIP SMLSALSVVR EKELGSIINL YVTPTTRSEF LLGKQLPYIA LGMLNFFLLC
GLSVFVFGVP HKGSFLTLTL AALLYIIIAT GMGLLISTFM KSQIAAIFGT AIITLIPATQ
FSGMIDPVAS LEGPGRWIGE VYPTSHFLTI ARGTFSKALD LTDLWQLFIP LLIAIPLVMG
LSILLLKKQE G
