A8F960 (SYE_BACP2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate--tRNA ligase
EC=6.1.1.17

Alternative name(s):
Glutamyl-tRNA synthetase
Short name=GluRS

Gene names

Name:	gltX
Ordered Locus Names:	BPUM_0077

Organism

Bacillus pumilus (strain SAFR-032) [Complete proteome] [HAMAP]

Taxonomic identifier

315750 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) By similarity. HAMAP MF_00022_B
Catalytic activity	ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu). HAMAP MF_00022_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00022_B
Subunit structure	Monomer By similarity. HAMAP MF_00022_B
Subcellular location	Cytoplasm HAMAP MF_00022_B.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 483	483	Glutamate--tRNA ligase HAMAP MF_00022_B		PRO_1000057191
Regions
	Motif	11 – 21	11	"HIGH" region HAMAP MF_00022_B
	Motif	252 – 256	5	"KMSKS" region HAMAP MF_00022_B
Sites
	Metal binding	108	1	Zinc By similarity
	Metal binding	110	1	Zinc By similarity
	Metal binding	135	1	Zinc By similarity
	Metal binding	137	1	Zinc By similarity
	Binding site	255	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A8F960 [UniParc]. Last modified November 13, 2007. Version 1. Checksum: A26ED8A92D61532A	FASTA	483	55,586
	10 20 30 40 50 60 MGNEVRVRYA PSPTGHLHIG NARTALFNYL FARSQGGKFI IRIEDTDQKR NVEGGEESQL 70 80 90 100 110 120 RHLQWLGIDW DESIDKDGGY GPYRQSERND IYKKYYDELL EKDLAYKCYC TAEELEEERE 130 140 150 160 170 180 AQIARSEMPR YSGKCSHLSK EEEDKLIAEG REPSIRFRVP KGEIIKFDDM VKGEISFETD 190 200 210 220 230 240 GIGDFVIVKK DGTPTYNFAV AVDDHLMKMT HILRGEDHIS NTPKQIMIFN AFGWDVPLFG 250 260 270 280 290 300 HMTLIVNENR KKLSKRDESI IQFIEQYKNL GYLPEALFNF IALLGWSPVG EEELFTKEQF 310 320 330 340 350 360 IDIFDVNRLS KSPALFDMHK LKWVNNQYVK ALDLDQVVAL TLPHLQKAGK VSEQLSDEKN 370 380 390 400 410 420 TWVRKLIALY HEQLSYGAEI VELTELFFKE QIEYNQEAKE VLAEEQVPEV MASFAGQLER 430 440 450 460 470 480 LESFTPDEIK AAIKAVQKET GHKGKKLFMP IRVAVTGQTH GPELPQSIEL LGKETVLNRI KQI

References

[1]

"Paradoxical DNA repair and peroxide resistance gene conservation in Bacillus pumilus SAFR-032." Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D., Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H., Lee S., Nazareth L., Blyth P., Holder M., Buhay C. , Tirumalai M.R., Liu Y., Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P., Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D., Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F., Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K., Weinstock G.M. PLoS ONE 2:E928-E928(2007) [PubMed: 17895969] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SAFR-032.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000813 Genomic DNA. Translation: ABV60777.1.
RefSeq	YP_001485337.1. NC_009848.1.
3D structure databases
ProteinModelPortal	A8F960.
ModBase	Search...
Protein-protein interaction databases
STRING	A8F960.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000063404; EBBACP00000061737; EBBACG00000063395.
GeneID	5619295.
GenomeReviews	Gene locus BPUM_0077 in contig CP000813_GR.
KEGG	bpu:BPUM_0077.
PATRIC	18963873. VBIBacPum16546_0081.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0008.
GeneTree	EBGT00050000002239.
HOGENOM	HBG628189.
OMA	DDFDMEI.
ProtClustDB	PRK01406.
Enzyme and pathway databases
BioCyc	BPUM315750:BPUM_0077-MONOMER.
Family and domain databases
HAMAP	MF_00022_B. Glu_tRNA_synth_B. [Tree]
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR004527. Glu-tRNA-synth_Ib_bac/mito. IPR000924. Glu/Gln-tRNA-synth_Ib. IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl. IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:1.10.1160.10. Glu/Gln-tRNA-synth_Ic_a-bdl. 1 hit. G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits. G3DSA:1.10.10.350. tRNA_synt_bd. 1 hit.
KO	K09698.
PANTHER	PTHR10119. Glu_tRNA-synt_1c. 1 hit. PTHR10119:SF1. PTHR10119:SF1. 1 hit.
Pfam	PF00749. tRNA-synt_1c. 1 hit. [Graphical view]
PRINTS	PR00987. TRNASYNTHGLU.
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00464. GltX_bact. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYE_BACP2

Accession

Primary (citable) accession number: A8F960

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	November 13, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program