GATB_STAAM
ID GATB_STAAM Reviewed; 475 AA.
AC P64201; Q99SY7;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE Short=Asp/Glu-ADT subunit B {ECO:0000255|HAMAP-Rule:MF_00121};
DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00121};
GN Name=gatB {ECO:0000255|HAMAP-Rule:MF_00121}; OrderedLocusNames=SAV1899;
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 Asn-tRNA(Asn) or
CC Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn)
CC or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-
CC tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the
CC presence of glutamine and ATP through an activated phospho-Asp-
CC tRNA(Asn) or phospho-Glu-tRNA(Gln). {ECO:0000255|HAMAP-Rule:MF_00121}.
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_00121};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-aspartyl-tRNA(Asn) + L-glutamine = ADP + 2 H(+)
CC + L-asparaginyl-tRNA(Asn) + L-glutamate + phosphate;
CC Xref=Rhea:RHEA:14513, Rhea:RHEA-COMP:9674, Rhea:RHEA-COMP:9677,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:78515, ChEBI:CHEBI:78516, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00121};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00121}.
CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00121}.
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DR EMBL; BA000017; BAB58061.1; -; Genomic_DNA.
DR RefSeq; WP_000545370.1; NC_002758.2.
DR PDB; 2DF4; X-ray; 3.20 A; B=1-475.
DR PDB; 2DQN; X-ray; 2.55 A; B=1-475.
DR PDB; 2F2A; X-ray; 2.30 A; B=1-475.
DR PDB; 2G5H; X-ray; 2.50 A; B=1-475.
DR PDB; 2G5I; X-ray; 3.35 A; B=1-475.
DR PDB; 3IP4; X-ray; 1.90 A; B=1-475.
DR PDBsum; 2DF4; -.
DR PDBsum; 2DQN; -.
DR PDBsum; 2F2A; -.
DR PDBsum; 2G5H; -.
DR PDBsum; 2G5I; -.
DR PDBsum; 3IP4; -.
DR AlphaFoldDB; P64201; -.
DR SMR; P64201; -.
DR World-2DPAGE; 0002:P64201; -.
DR PaxDb; P64201; -.
DR EnsemblBacteria; BAB58061; BAB58061; SAV1899.
DR KEGG; sav:SAV1899; -.
DR HOGENOM; CLU_019240_0_0_9; -.
DR OMA; ARKWWMG; -.
DR PhylomeDB; P64201; -.
DR BioCyc; SAUR158878:SAV_RS10405-MON; -.
DR BRENDA; 6.3.5.7; 3352.
DR EvolutionaryTrace; P64201; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:RHEA.
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 HAMAP; MF_00121; GatB; 1.
DR InterPro; IPR004413; Apn/Gln-ADT_bsu.
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; IPR042114; GatB_C_1.
DR InterPro; IPR023168; GatB_Yqey_C_2.
DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11659; PTHR11659; 1.
DR Pfam; PF02934; GatB_N; 1.
DR Pfam; PF02637; GatB_Yqey; 1.
DR SMART; SM00845; GatB_Yqey; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR SUPFAM; SSF89095; SSF89095; 1.
DR TIGRFAMs; TIGR00133; gatB; 1.
DR PROSITE; PS01234; GATB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..475
FT /note="Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase
FT subunit B"
FT /id="PRO_0000148834"
FT STRAND 3..14
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 39..43
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 114..125
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 142..145
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 160..177
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 188..199
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2F2A"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 217..237
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 255..261
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:2DF4"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:2DF4"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 347..354
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 366..377
FT /evidence="ECO:0007829|PDB:3IP4"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2F2A"
FT HELIX 383..396
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 400..405
FT /evidence="ECO:0007829|PDB:3IP4"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 430..437
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 443..454
FT /evidence="ECO:0007829|PDB:3IP4"
FT HELIX 461..474
FT /evidence="ECO:0007829|PDB:3IP4"
SQ SEQUENCE 475 AA; 53657 MW; 96805EE591658154 CRC64;
MHFETVIGLE VHVELKTDSK MFSPSPAHFG AEPNSNTNVI DLAYPGVLPV VNKRAVDWAM
RAAMALNMEI ATESKFDRKN YFYPDNPKAY QISQFDQPIG ENGYIDIEVD GETKRIGITR
LHMEEDAGKS THKGEYSLVD LNRQGTPLIE IVSEPDIRSP KEAYAYLEKL RSIIQYTGVS
DVKMEEGSLR CDANISLRPY GQEKFGTKAE LKNLNSFNYV RKGLEYEEKR QEEELLNGGE
IGQETRRFDE STGKTILMRV KEGSDDYRYF PEPDIVPLYI DDAWKERVRQ TIPELPDERK
AKYVNELGLP AYDAHVLTLT KEMSDFFEST IEHGADVKLT SNWLMGGVNE YLNKNQVELL
DTKLTPENLA GMIKLIEDGT MSSKIAKKVF PELAAKGGNA KQIMEDNGLV QISDEATLLK
FVNEALDNNE QSVEDYKNGK GKAMGFLVGQ IMKASKGQAN PQLVNQLLKQ ELDKR
