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Database: UniProt
Entry: Q87S73_VIBPA
LinkDB: Q87S73_VIBPA
Original site: Q87S73_VIBPA 
ID   Q87S73_VIBPA            Unreviewed;       555 AA.
AC   Q87S73;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Energy-dependent translational throttle protein EttA {ECO:0000256|HAMAP-Rule:MF_00847};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00847};
DE   AltName: Full=Translational regulatory factor EttA {ECO:0000256|HAMAP-Rule:MF_00847};
GN   Name=ettA {ECO:0000256|HAMAP-Rule:MF_00847};
GN   OrderedLocusNames=VP0551 {ECO:0000313|EMBL:BAC58814.1};
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC58814.1, ECO:0000313|Proteomes:UP000002493};
RN   [1] {ECO:0000313|EMBL:BAC58814.1, ECO:0000313|Proteomes:UP000002493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX   PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00847}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00847}.
CC       Note=Associates with ribosomes and polysomes. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00847}.
CC   -!- DOMAIN: The arm domain is inserted in the first ABC transporter domain.
CC       Probably contacts ribosomal protein L1. {ECO:0000256|HAMAP-
CC       Rule:MF_00847}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC       Translational throttle EttA subfamily. {ECO:0000256|ARBA:ARBA00005868,
CC       ECO:0000256|HAMAP-Rule:MF_00847}.
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DR   EMBL; BA000031; BAC58814.1; -; Genomic_DNA.
DR   RefSeq; NP_796930.1; NC_004603.1.
DR   RefSeq; WP_005460278.1; NC_004603.1.
DR   AlphaFoldDB; Q87S73; -.
DR   GeneID; 1188019; -.
DR   KEGG; vpa:VP0551; -.
DR   PATRIC; fig|223926.6.peg.523; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_6; -.
DR   OMA; VSYKPQY; -.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd03221; ABCF_EF-3; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR03719; ABC_ABC_ChvD; 1.
DR   PANTHER; PTHR43858; ENERGY-DEPENDENT TRANSLATIONAL THROTTLE PROTEIN ETTA; 1.
DR   PANTHER; PTHR43858:SF1; NON-TRANSPORTER ABC PROTEIN; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   Pfam; PF12848; ABC_tran_Xtn; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00847}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00847};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00847};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00847}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00847};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002493};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00847};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00847};
KW   rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP-
KW   Rule:MF_00847};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_00847};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_00847}.
FT   DOMAIN          6..259
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          324..542
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          95..139
FT                   /note="Arm"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT   REGION          242..322
FT                   /note="PtIM"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
FT   BINDING         356..363
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00847"
SQ   SEQUENCE   555 AA;  62246 MW;  9A2308F6C47FC988 CRC64;
     MAEYVYTMSR VSKIVPPKRQ ILKDISLSFF PGAKIGVLGL NGAGKSTLLR IMAGIDTDID
     GEARPQPGLN VGYLPQEPVL DESKTVREVV EEAVADVADA LKRLDAVYAA YAEPDADFDA
     LAKEQGELEA LIQAKDGHNL ENTLERAADA LRLPEWDQKI AHLSGGERRR VAICRLLLSK
     PDMLLLDEPT NHLDAESVAW LERFLVDYSG TVVAITHDRY FLDNAAGWIL ELDRGEGIPW
     EGNYTSWLEQ KDARLQQEAS QESARQKTIE KELEWVRKNP KGRQAKSKAR MARFEELQNT
     EHQKRNETNE LFIPPGERLG DKVIEVKNLT KSFDGRVLID DLSFNMPKGA IVGIIGANGA
     GKSTLFKMLS GTEQPDSGTI EMGDTVKLAS VEQFRDSMND KNTVFQEISE GADIIKINNF
     EIPARAYCSR FNFKGSDQQK VIGELSGGER NRVHLAKLLK AGGNVLLLDE PTNDLDVETL
     RALEEALLEF PGCAMVISHD RWFLDRIATH IIDYRDEGQV NFYEGNYTEY MDWLKKTLGP
     EAAEPHRIKY KRIAK
//
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