A7GT67 (SYA_BACCN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS

Gene names

Name:	alaS
Ordered Locus Names:	Bcer98_3101

Organism

Bacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]

Taxonomic identifier

315749 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	880 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP MF_00036_B
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036_B
Cofactor	Binds 1 zinc ion per subunit By similarity. HAMAP MF_00036_B
Subcellular location	Cytoplasm By similarity HAMAP MF_00036_B.
Domain	Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP MF_00036_B
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	alanyl-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 alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA 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 – 880	880	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000347498
Sites
	Metal binding	567	1	Zinc Potential
	Metal binding	571	1	Zinc Potential
	Metal binding	669	1	Zinc Potential
	Metal binding	673	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	A7GT67 [UniParc]. Last modified September 11, 2007. Version 1. Checksum: D8E4464B4AA3CF73	FASTA	880	97,156
	10 20 30 40 50 60 MKQLTGAQIR QMFLDFFKEK GHAIEPSASL VPHEDPSLLW INSGVATLKK YFDGRVIPQN 70 80 90 100 110 120 PRITNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAITWAWE FLTSDKWIGF 130 140 150 160 170 180 DKELLSVTIH PEDEEAFTIW HEKIGVPKER IIRLEENFWD IGEGPSGPNT EIFYDRGEAY 190 200 210 220 230 240 GNDPSDPELY PGGENERYLE VWNLVFSQFN HNPDGSYTPL PKKNIDTGMG LERMTSIVQN 250 260 270 280 290 300 VPTNFDTDLF MPMIGATESI SGEKYRSGDA EKDMAFKVIA DHIRTVTFAV GDGALPSNEG 310 320 330 340 350 360 RGYVLRRLLR RAVRYAKKLN MNRPFMYELV PVVGEVMKDF YPEVLEKKDF IAKVVKNEEE 370 380 390 400 410 420 RFHETLHDGE AILAEVIAKA KEEKTTVISG VDAFRLYDTY GFPVELTEEY AEEAGMTVDH 430 440 450 460 470 480 AGFEAEMEKQ RERARAARQD VDSMQVQGGV LGEIKVASEF VGYGTVATES NVVALVKNGE 490 500 510 520 530 540 YTDSLQAGEE GQLMLDVTPF YAESGGQIAD SGYLLTDGVK VLVKDVQKAP NGQNLHKVVV 550 560 570 580 590 600 EEGVLTKDAT VKAVIDTKNR SSIVKNHTAT HLLHQALKDV LGTHVNQAGS LVTAERLRFD 610 620 630 640 650 660 FSHFGQVQAD ELEKIERIVN EKIWESIDVE ISQKAIEEAK EMGAMALFGE KYGDVVRVVQ 670 680 690 700 710 720 VGDYSLELCG GCHVDNTASI GIFKIVAESG IGAGTRRIEA VTGKAAYELM NDQVSLLKEA 730 740 750 760 770 780 AGKMKTNPKD ILTRVDGLFA EVKQLQKENE SLAAKLSNIE AGNLTDAVVS VDGINVLATK 790 800 810 820 830 840 VNVADMNNLR TMMDDLKNKL ESAVIVLAAV NDDKVNILAG VTKDLVGQGY HAGKLVKEVA 850 860 870 880 SRCGGGGGGR PDMAQAGGKN PAQVDEALAF VQEYVKSVSK

References

[1]

"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity." Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A. Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NVH 391-98.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000764 Genomic DNA. Translation: ABS23325.1.
RefSeq	YP_001376320.1. NC_009674.1.
3D structure databases
ProteinModelPortal	A7GT67.
ModBase	Search...
Protein-protein interaction databases
STRING	A7GT67.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000038765; EBBACP00000037816; EBBACG00000038756.
GeneID	5344187.
GenomeReviews	Gene locus Bcer98_3101 in contig CP000764_GR.
KEGG	bcy:Bcer98_3101.
PATRIC	18934832. VBIBacCyt128034_3259.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0013.
GeneTree	EBGT00050000001776.
HOGENOM	HBG354397.
OMA	VILEMES.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	BCER315749:BCER98_3101-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018162. Ala-tRNA-synth_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_synth_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
KO	K01872.
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00344. AlaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_BACCN

Accession

Primary (citable) accession number: A7GT67

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 2, 2008
Last sequence update:	September 11, 2007
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program