GATA_STAAM
ID GATA_STAAM Reviewed; 485 AA.
AC P63488; Q99SY6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120}; OrderedLocusNames=SAV1900;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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). {ECO:0000255|HAMAP-Rule:MF_00120}.
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; EC=6.3.5.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00120};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00120}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00120}.
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DR EMBL; BA000017; BAB58062.1; -; Genomic_DNA.
DR RefSeq; WP_000027919.1; NC_002758.2.
DR PDB; 2DF4; X-ray; 3.20 A; A=1-485.
DR PDB; 2DQN; X-ray; 2.55 A; A=1-485.
DR PDB; 2F2A; X-ray; 2.30 A; A=1-485.
DR PDB; 2G5H; X-ray; 2.50 A; A=1-485.
DR PDB; 2G5I; X-ray; 3.35 A; A=1-485.
DR PDB; 3IP4; X-ray; 1.90 A; A=1-485.
DR PDBsum; 2DF4; -.
DR PDBsum; 2DQN; -.
DR PDBsum; 2F2A; -.
DR PDBsum; 2G5H; -.
DR PDBsum; 2G5I; -.
DR PDBsum; 3IP4; -.
DR AlphaFoldDB; P63488; -.
DR SMR; P63488; -.
DR World-2DPAGE; 0002:P63488; -.
DR PaxDb; P63488; -.
DR EnsemblBacteria; BAB58062; BAB58062; SAV1900.
DR KEGG; sav:SAV1900; -.
DR HOGENOM; CLU_009600_0_3_9; -.
DR OMA; EVSCPHF; -.
DR PhylomeDB; P63488; -.
DR BioCyc; SAUR158878:SAV_RS10410-MON; -.
DR BRENDA; 6.3.5.7; 3352.
DR EvolutionaryTrace; P63488; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; 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; 3.90.1300.10; -; 1.
DR HAMAP; MF_00120; GatA; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR020556; Amidase_CS.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR004412; GatA.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..485
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105199"
FT ACT_SITE 79
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 178
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 8..16
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 22..40
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 106..113
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 156..163
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2DF4"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 305..320
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 325..330
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 353..366
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 368..374
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 375..393
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 397..407
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 429..434
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 462..475
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3IP4"
SQ SEQUENCE 485 AA; 52801 MW; 52F78A35E4863965 CRC64;
MSIRYESVEN LLTLIKDKKI KPSDVVKDIY DAIEETDPTI KSFLALDKEN AIKKAQELDE
LQAKDQMDGK LFGIPMGIKD NIITNGLETT CASKMLEGFV PIYESTVMEK LHKENAVLIG
KLNMDEFAMG GSTETSYFKK TVNPFDHKAV PGGSSGGSAA AVAAGLVPLS LGSDTGGSIR
QPAAYCGVVG MKPTYGRVSR FGLVAFASSL DQIGPLTRNV KDNAIVLEAI SGADVNDSTS
APVDDVDFTS EIGKDIKGLK VALPKEYLGE GVADDVKEAV QNAVETLKSL GAVVEEVSLP
NTKFGIPSYY VIASSEASSN LSRFDGIRYG YHSKEAHSLE ELYKMSRSEG FGKEVKRRIF
LGTFALSSGY YDAYYKKSQK VRTLIKNDFD KVFENYDVVV GPTAPTTAFN LGEEIDDPLT
MYANDLLTTP VNLAGLPGIS VPCGQSNGRP IGLQFIGKPF DEKTLYRVAY QYETQYNLHD
VYEKL
