ETTA_MYCTU
ID ETTA_MYCTU Reviewed; 558 AA.
AC P9WQK3; L0T9X4; O53204; Q7D727;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Energy-dependent translational throttle protein EttA {ECO:0000255|HAMAP-Rule:MF_00847};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00847};
DE AltName: Full=Translational regulatory factor EttA {ECO:0000255|HAMAP-Rule:MF_00847};
GN Name=ettA {ECO:0000255|HAMAP-Rule:MF_00847}; OrderedLocusNames=Rv2477c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP INDUCTION.
RX PubMed=20001742; DOI=10.1089/mdr.2009.0054;
RA Gupta A.K., Katoch V.M., Chauhan D.S., Sharma R., Singh M., Venkatesan K.,
RA Sharma V.D.;
RT "Microarray analysis of efflux pump genes in multidrug-resistant
RT Mycobacterium tuberculosis during stress induced by common anti-tuberculous
RT drugs.";
RL Microb. Drug Resist. 16:21-28(2010).
RN [3]
RP PUPYLATION AT LYS-338, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: A translation factor that gates the progression of the 70S
CC ribosomal initiation complex (IC, containing tRNA(fMet) in the P-site)
CC into the translation elongation cycle by using a mechanism sensitive to
CC the ATP/ADP ratio. Binds to the 70S ribosome E-site where it modulates
CC the state of the translating ribosome during subunit translocation. ATP
CC hydrolysis probably frees it from the ribosome, which can enter the
CC elongation phase. {ECO:0000255|HAMAP-Rule:MF_00847}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00847};
CC -!- SUBUNIT: Monomer. Probably contacts ribosomal proteins L1, L5, L33 and
CC S7, the 16S and 23S rRNA and the P-site containing tRNA(fMet).
CC {ECO:0000255|HAMAP-Rule:MF_00847}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00847}.
CC Note=Associates with ribosomes and polysomes. {ECO:0000255|HAMAP-
CC Rule:MF_00847}.
CC -!- INDUCTION: Induced by ofloxacin stress. {ECO:0000269|PubMed:20001742}.
CC -!- DOMAIN: The arm domain is inserted in the first ABC transporter domain.
CC Probably contacts ribosomal protein L1. {ECO:0000255|HAMAP-
CC Rule:MF_00847}.
CC -!- DOMAIN: The P-site tRNA interaction motif (PtIM domain) probably
CC interacts with the P-site tRNA(fMet) as well as the 23S rRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00847}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC Translational throttle EttA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00847, ECO:0000305}.
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DR EMBL; AL123456; CCP45271.1; -; Genomic_DNA.
DR PIR; D70867; D70867.
DR RefSeq; NP_216993.1; NC_000962.3.
DR RefSeq; WP_003412708.1; NZ_NVQJ01000024.1.
DR PDB; 7MSC; EM; 2.97 A; x=1-558.
DR PDB; 7MSH; EM; 3.23 A; x=1-558.
DR PDB; 7MSM; EM; 2.79 A; x=1-558.
DR PDB; 7MSZ; EM; 3.10 A; x=1-558.
DR PDB; 7MU0; X-ray; 2.90 A; A/B=1-558.
DR PDBsum; 7MSC; -.
DR PDBsum; 7MSH; -.
DR PDBsum; 7MSM; -.
DR PDBsum; 7MSZ; -.
DR PDBsum; 7MU0; -.
DR AlphaFoldDB; P9WQK3; -.
DR SMR; P9WQK3; -.
DR STRING; 83332.Rv2477c; -.
DR TCDB; 3.A.1.120.8; the atp-binding cassette (abc) superfamily.
DR PaxDb; P9WQK3; -.
DR DNASU; 887757; -.
DR GeneID; 45426470; -.
DR GeneID; 887757; -.
DR KEGG; mtu:Rv2477c; -.
DR TubercuList; Rv2477c; -.
DR eggNOG; COG0488; Bacteria.
DR OMA; ISYKPQY; -.
DR PhylomeDB; P9WQK3; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045900; P:negative regulation of translational elongation; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00847; EttA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR022374; EttA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43858; PTHR43858; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03719; ABC_ABC_ChvD; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding; rRNA-binding; Translation regulation; tRNA-binding;
KW Ubl conjugation.
FT CHAIN 1..558
FT /note="Energy-dependent translational throttle protein
FT EttA"
FT /id="PRO_0000395861"
FT DOMAIN 6..256
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT DOMAIN 322..552
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT REGION 94..136
FT /note="Arm"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT REGION 239..320
FT /note="PtIM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00847"
FT CROSSLNK 338
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
SQ SEQUENCE 558 AA; 61893 MW; 1B2E6E600C4FDD8A CRC64;
MAEFIYTMKK VRKAHGDKVI LDDVTLSFYP GAKIGVVGPN GAGKSSVLRI MAGLDKPNNG
DAFLATGATV GILQQEPPLN EDKTVRGNVE EGMGDIKIKL DRFNEVAELM ATDYTDELME
EMGRLQEELD HADAWDLDAQ LEQAMDALRC PPADEPVTNL SGGERRRVAL CKLLLSKPDL
LLLDEPTNHL DAESVQWLEQ HLASYPGAIL AVTHDRYFLD NVAEWILELD RGRAYPYEGN
YSTYLEKKAE RLAVQGRKDA KLQKRLTEEL AWVRSGAKAR QAKSKARLQR YEEMAAEAEK
TRKLDFEEIQ IPVGPRLGNV VVEVDHLDKG YDGRALIKDL SFSLPRNGIV GVIGPNGVGK
TTLFKTIVGL ETPDSGSVKV GETVKLSYVD QARAGIDPRK TVWEVVSDGL DYIQVGQTEV
PSRAYVSAFG FKGPDQQKPA GVLSGGERNR LNLALTLKQG GNLILLDEPT NDLDVETLGS
LENALLNFPG CAVVISHDRW FLDRTCTHIL AWEGDDDNEA KWFWFEGNFG AYEENKVERL
GVDAARPHRV THRKLTRG
