Q65GS5 (SYA_BACLD) 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:	BLi02869, BL02033

Organism

Bacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]

Taxonomic identifier

279010 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	878 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 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 – 878	878	Alanine--tRNA ligase HAMAP MF_00036_B		PRO_0000075056
Sites
	Metal binding	566	1	Zinc Potential
	Metal binding	570	1	Zinc Potential
	Metal binding	668	1	Zinc Potential
	Metal binding	672	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q65GS5 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: 02FC6488B0864F87	FASTA	878	97,670
	10 20 30 40 50 60 MKTLTSAQVR QMFLDFFKEK GHAVEPSASL IPHEDPSLLW INSGVATLKK YFDGRVVPEN 70 80 90 100 110 120 PRICNAQKSI RTNDIENVGK TARHHTFFEM LGNFSIGDYF KEEAIEWAWE FLTDQKWIGF 130 140 150 160 170 180 DPERLSVTVH PEDDEAYELW SKKIGIPEER IIRLEGNFWD IGEGPSGPNT EIFYDRGEDY 190 200 210 220 230 240 GNDPSDPELY PGGENERYLE VWNLVFSEFN HNPDGTYTPL PKKNIDTGMG LERMVSVIQD 250 260 270 280 290 300 AKTNYDTDLF MPIIKATEAI SGEKYGTSAE KDTAFKVVAD HIRTAAFAVG DGALPSNEGR 310 320 330 340 350 360 GYVIRRLLRR AVRYAKSINI NRPFMYELVP VVADIMAAFY GEVKEKADFI AKVIKTEEER 370 380 390 400 410 420 FHETLHEGLA ILSEVIQKEK AKGNRIISGE DVFKLYDTYG FPVELTEEYA EDEGMEVDHE 430 440 450 460 470 480 GFEREMDKQR ERARQARQDV GSMQVQGGAL RDIMTESEFI GYSDIKTETK IAELLQDGEL 490 500 510 520 530 540 VDLVQEGQKV QFILEKTPFY AESGGQIGDK GWVKSGDAAI RVTDVKKAPN GQHLHEGIVE 550 560 570 580 590 600 SGAIKKGMSV TAEVTERLRK DIVKNHTATH LLHQALKDVL GTHVNQAGSL VTDSRLRFDF 610 620 630 640 650 660 SHFGQVTKEE LEQIETKVNE KIWASIPVQI DLKPIAEAKA MGAMALFGEK YGDIVRVVQV 670 680 690 700 710 720 GDYSIELCGG CHVRNTAEIG LFKIVSESGI GAGTRRIEAV TGQGAYEEMN AKLELLEQAA 730 740 750 760 770 780 EVLKTNVKEV PKRIEALQSD LKDAQRENES LLAKLGNKEA GEILEKVKEI DGIKLLAEKV 790 800 810 820 830 840 NAKDMNHLRT MVDDLKAKLG SAVIVLGAVQ NEKVNISAGV TKDLIERGFH AGKLVKQVAE 850 860 870 ACGGGGGGRP DMAQAGGKQP ERLAEALASA EEWVKSVL

References

[1]

"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential." Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G. J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

[2]

"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species." Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. , Galleron N., Ehrlich S.D., Berka R.M. Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017333 Genomic DNA. Translation: AAU41739.1. CP000002 Genomic DNA. Translation: AAU24375.1.
RefSeq	YP_080013.1. NC_006270.3. YP_092432.1. NC_006322.1.
3D structure databases
ProteinModelPortal	Q65GS5.
ModBase	Search...
Protein-protein interaction databases
STRING	Q65GS5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000054917; EBBACP00000053448; EBBACG00000054908. EBBACT00000062410; EBBACP00000060843; EBBACG00000062401.
GeneID	3027711. 3098156.
GenomeReviews	Gene locus BLi02869 in contig AE017333_GR. Gene locus BL02033 in contig CP000002_GR.
KEGG	bld:BLi02869. bli:BL02033.
NMPDR	fig|279010.5.peg.3198.
PATRIC	18951452. VBIBacLic203714_2927.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0013.
GeneTree	EBGT00050000001776.
HOGENOM	HBG354397.
OMA	GESKTDQ.
PhylomeDB	Q65GS5.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	BLIC279010-1:BLI02869-MONOMER. BLIC279010:BL02033-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_BACLD

Accession

Primary (citable) accession number: Q65GS5
Secondary accession number(s): Q62S84

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	October 25, 2004
Last modified:	January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program