ID   GATE_SULAC              Reviewed;         634 AA.
AC   Q4J945;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit E {ECO:0000255|HAMAP-Rule:MF_00588};
DE            Short=Glu-ADT subunit E {ECO:0000255|HAMAP-Rule:MF_00588};
DE            EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00588};
GN   Name=gatE {ECO:0000255|HAMAP-Rule:MF_00588}; OrderedLocusNames=Saci_1350;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC       which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC       presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC       tRNA(Gln). The GatDE system is specific for glutamate and does not act
CC       on aspartate. {ECO:0000255|HAMAP-Rule:MF_00588}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00588};
CC   -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP-
CC       Rule:MF_00588}.
CC   -!- SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00588}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY80685.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000077; AAY80685.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015385605.1; NC_007181.1.
DR   AlphaFoldDB; Q4J945; -.
DR   SMR; Q4J945; -.
DR   STRING; 330779.Saci_1350; -.
DR   PRIDE; Q4J945; -.
DR   EnsemblBacteria; AAY80685; AAY80685; Saci_1350.
DR   GeneID; 3473463; -.
DR   KEGG; sai:Saci_1350; -.
DR   PATRIC; fig|330779.12.peg.1303; -.
DR   eggNOG; arCOG01719; Archaea.
DR   HOGENOM; CLU_030702_0_0_2; -.
DR   Proteomes; UP000001018; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.10.410; -; 1.
DR   Gene3D; 1.10.150.380; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   HAMAP; MF_00588; GatE; 1.
DR   InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E.
DR   InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat.
DR   InterPro; IPR018027; Asn/Gln_amidotransferase.
DR   InterPro; IPR003789; Asn/Gln_tRNA_amidoTrase-B-like.
DR   InterPro; IPR004115; GAD-like_sf.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR042114; GatB_C_1.
DR   InterPro; IPR023168; GatB_Yqey_C_2.
DR   InterPro; IPR004414; GatE.
DR   InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   PANTHER; PTHR11659; PTHR11659; 1.
DR   PANTHER; PTHR11659:SF2; PTHR11659:SF2; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF02934; GatB_N; 1.
DR   Pfam; PF02637; GatB_Yqey; 1.
DR   SMART; SM00845; GatB_Yqey; 1.
DR   SUPFAM; SSF55261; SSF55261; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   SUPFAM; SSF89095; SSF89095; 1.
DR   TIGRFAMs; TIGR00134; gatE_arch; 1.
DR   PROSITE; PS01234; GATB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..634
FT                   /note="Glutamyl-tRNA(Gln) amidotransferase subunit E"
FT                   /id="PRO_0000140081"
SQ   SEQUENCE   634 AA;  71325 MW;  CA0D3F03743C799D CRC64;
     MTELDYSKLG LKVGLEIHQQ LNTNKKLFCD CSTTLDEKHH GTLQRYLRPS FSEIGEIDTA
     ALFEWQKGKK YLYQIPFNSC LVEADEEPPH GLNREALAVV LAVAMSLESN IVDEIYVMRK
     IVIDGSDTTG FQRTSIVAMG GQVIVEGKKI GIQTIALEED AARKISESAN ETMYSLDRLG
     IPLIEISTAP DITTPEEAEK VAFRIGQLLR LTGKVKRGIG TIRQDLNVSI QGGVKTEIKG
     VQRLELIPEI IKNEARRQYE LLKIKDELVN KRGLSKTIVE NEIKELELTH LFRNTNSKII
     KKELEKGGLI YGIKFKGFKG IFGRELMPNR RFGTEIADYV RALAELGGIF HSDELPNYGI
     TSEEVESVKK ELGIGENDGF VLVIGDKEKL KVAITKIKER VLYAFVGVPK ETRVALDDGT
     TKFMRPQPGS ARMYPETDII PIKIDESILN FAKSFVPENP ETKLRKLIEM GLSKELATEI
     LNSPRLDLFE ELSKKYSPKV SPIVIATTLE NYIKYAKSKG GDISVITDEV IEEIINALYN
     DKISKDSIQE ILVDYSTSKK PIRNIVDNYA KITDEELNRI IDKILDENKD IINQKGEKAF
     NVIIGKVMNV VKGRAEGKKV VDTLKLKMKN YPRT