A0REI7 (A0REI7_BACAH) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Lysine--tRNA ligase HAMAP-Rule MF_00177
EC=6.1.1.6 HAMAP-Rule MF_00177

Alternative name(s):
Lysyl-tRNA synthetase HAMAP-Rule MF_00177

Gene names

Name:	lysS HAMAP-Rule MF_00177
Ordered Locus Names:	BALH_2333 EMBL ABK85630.1

Organism

Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP] EMBL ABK85630.1

Taxonomic identifier

412694 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › Bacillus thuringiensis

Protein attributes

Sequence length	517 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). HAMAP-Rule MF_00177
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00177.
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family. HAMAP-Rule MF_00177 RuleBase RU003489

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP-Rule MF_00177 RuleBase RU003489
Cellular component	Cytoplasm HAMAP-Rule MF_00177
Ligand	ATP-binding HAMAP-Rule MF_00177 RuleBase RU003489 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP-Rule MF_00177 RuleBase RU003489 EMBL ABK85630.1 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	lysyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP lysine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Regions
	Motif	29 – 37	9	"HIGH" region By similarity HAMAP-Rule MF_00177
	Motif	281 – 285	5	"KMSKS" region By similarity HAMAP-Rule MF_00177

Sequences

	Sequence		Length	Mass (Da)
	A0REI7 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 52693F023EA0B835	FASTA	517	60,938
	10 20 30 40 50 60 MHWAYEVALE LIRKHPNKET FVCASGISPS GSVHIGNFRE IVTTYFVVRA LQDLGKKTRF 70 80 90 100 110 120 IFSWDDYDRF RKVPKNIDPS FVKYIGMPYC DIPDPYGCHN SYAEHFEKEF EKSLQAFGIE 130 140 150 160 170 180 VEFIYQHDEY RNGRYNKSIL EALYKRKEIY DVLMDFKTGE CSEEERERFY PVTLYCERCG 190 200 210 220 230 240 KDTTTITHFD EALKTVRYEC ECGNQNELSI LNTNKMKLNW KIDWPMRWMI EDVIFEPGGR 250 260 270 280 290 300 DHSSETGSYN VSKEIARKIF NREAPHYVAY DFIGIKGNHE KMSSSSGNSI TPSELLKVYL 310 320 330 340 350 360 PEVILFMFAK YRPNAAFHIS LDEDVIRNYT EYERLKGSYE NKTLKNEDLF DAIKLSRAEN 370 380 390 400 410 420 GFKEYPKFNQ VAGTLPLLHF DSFILQGILE KIDRSYGLDE MKSISNRAEY WIRKFQSEKL 430 440 450 460 470 480 IEVNQEKNTE FYNTLDKSQK EWLVEVCEIL RSNKDYSNIM EQLYSICHHE NKKIMKENQK 490 500 510 QLFTIIYMLI INQSNGPRIP LLIHVVGIEK SIALLDF

References

[1]

"The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. , Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S. J. Bacteriol. 189:3680-3681(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Al Hakam EMBL ABK85630.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000485 Genomic DNA. Translation: ABK85630.1.
RefSeq	YP_895137.1. NC_008600.1.
3D structure databases
ProteinModelPortal	A0REI7.
ModBase	Search...
Protein-protein interaction databases
STRING	412694.BALH_2333.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK85630; ABK85630; BALH_2333.
GeneID	4544407.
KEGG	btl:BALH_2333.
PATRIC	18997226. VBIBacThu63319_2613.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1384.
HOGENOM	HOG000226938.
KO	K04566.
OMA	FIFSWDD.
ProtClustDB	PRK00750.
Enzyme and pathway databases
BioCyc	BTHU412694:GH1W-2322-MONOMER.
Family and domain databases
Gene3D	1.10.10.350. 1 hit. 2.30.30.300. 1 hit. 3.40.50.620. 2 hits.
HAMAP	MF_00177. Lys_tRNA_synth_class1.
InterPro	IPR008925. aa-tRNA-synth_I_codon-bd. IPR020751. aa-tRNA-synth_I_codon-bd_sub2. IPR001412. aa-tRNA-synth_I_CS. IPR002904. Lys-tRNA-ligase. IPR023386. Lys-tRNA-ligase_insertion. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF01921. tRNA-synt_1f. 1 hit. [Graphical view]
SUPFAM	SSF48163. tRNA-synt_bind. 1 hit.
TIGRFAMs	TIGR00467. lysS_arch. 1 hit.
PROSITE	PS00178. AA_TRNA_LIGASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

A0REI7_BACAH

Accession

Primary (citable) accession number: A0REI7

Entry history

Integrated into UniProtKB/TrEMBL:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	May 29, 2013
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)