ECOLI:SYA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	alaS (synonyms: lovB)
Protein Name(s)	Alanine--tRNA ligase Alanyl-tRNA synthetase AlaRS
External Links
UniProt	P00957
EMBL	U00096 AP009048 J01581 L07596 D44453 Z28405
PIR	E65049
RefSeq	NP_417177.1 YP_490906.1
PDB	3HXU 3HXV 3HXW 3HXX 3HXY 3HXZ 3HY0 3HY1
PDBsum	3HXU 3HXV 3HXW 3HXX 3HXY 3HXZ 3HY0 3HY1
ProteinModelPortal	P00957
SMR	P00957
BioGrid	851507
DIP	DIP-9080N
IntAct	P00957
MINT	MINT-1266342
STRING	511145.b2697
MoonProt	P00957
SWISS-2DPAGE	P00957
PaxDb	P00957
PRIDE	P00957
EnsemblBacteria	AAC75739 BAA16559
GeneID	12932289 947175
KEGG	ecj:Y75_p2635 eco:b2697
PATRIC	32120790
EchoBASE	EB0033
EcoGene	EG10034
eggNOG	COG0013
HOGENOM	HOG000156964
InParanoid	P00957
KO	K01872
OMA	PCSEIHI
OrthoDB	EOG6Q2SQ2
PhylomeDB	P00957
BioCyc	EcoCyc:ALAS-MONOMER ECOL316407:JW2667-MONOMER MetaCyc:ALAS-MONOMER
EvolutionaryTrace	P00957
PRO	PR:P00957
Proteomes	UP000000318 UP000000625
Genevestigator	P00957
GO	GO:0005829 GO:0016020 GO:0004813 GO:0002161 GO:0005524 GO:0001141 GO:0042802 GO:0000049 GO:0008270 GO:0006419 GO:0045892 GO:0006450
HAMAP	MF_00036_B
InterPro	IPR002318 IPR018162 IPR018165 IPR018164 IPR023033 IPR003156 IPR018163 IPR009000 IPR012947
Pfam	PF02272 PF01411 PF07973
PRINTS	PR00980
SMART	SM00863
SUPFAM	SSF101353 SSF50447 SSF55186
TIGRFAMs	TIGR00344
PROSITE	PS50860

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0006816	calcium ion transport	PMID:383694^[1]	ECO:0000315			P		Fig 1. Mutants sensitive to growth inhibition by CaCl2 were found to have alterations in calcium uptake in everted membrane vesicles. These mutations map at different loci on the Escherichia coli chromosomes. A mutation at the calA locus results in vesicles which have two- to threefold higher levels of uptake activity than vesicles from wild-type cells. The calA mutation is phenotypically expressed as increased sensitivity to CaCl2 in a strain also harboring a mutation in the corA locus, which is involved in Mg2+ transport.	complete CACAO 4713
part_of	GO:0016020	membrane	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16858726^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002161	aminoacyl-tRNA editing activity	PMID:12554667^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002161	aminoacyl-tRNA editing activity	PMID:18172502^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10034 PANTHER:PTN000207080	P		Seeded From UniProt	complete
enables	GO:0016597	amino acid binding	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000206950 RGD:1304832	F		Seeded From UniProt	complete
involved_in	GO:0006419	alanyl-tRNA aminoacylation	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10034 MGI:MGI:2384560 PANTHER:PTN000206950 RGD:1304832 SGD:S000005862 UniProtKB:P49588	P		Seeded From UniProt	complete
involved_in	GO:0006400	tRNA modification	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2384560 PANTHER:PTN000206950	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10034 PANTHER:PTN000207063 UniProtKB:P9WFW7	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000206950 RGD:1304832	F		Seeded From UniProt	complete
enables	GO:0004813	alanine-tRNA ligase activity	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10034 MGI:MGI:2384560 PANTHER:PTN000206950 RGD:1304832 SGD:S000005862 UniProtKB:P49588 UniProtKB:Q5JTZ9	F		Seeded From UniProt	complete
enables	GO:0002161	aminoacyl-tRNA editing activity	PMID:21873635^[5]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10034 MGI:MGI:2384560 PANTHER:PTN000206950 UniProtKB:P49588 UniProtKB:Q57984	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16858726^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P00957	F	occurs_in:(GO:0005737)	Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:6264314^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:1712632^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006419	alanyl-tRNA aminoacylation	PMID:7005211^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:15911532^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004813	alanine-tRNA ligase activity	PMID:7005211^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002196	Ser-tRNA(Ala) hydrolase activity	PMID:6117825^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002196	Ser-tRNA(Ala) hydrolase activity	PMID:18172502^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0001217	DNA-binding transcription repressor activity	PMID:6264314^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0106074	aminoacyl-tRNA metabolism involved in translational fidelity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0002161	P		Seeded From UniProt	complete
involved_in	GO:0106074	aminoacyl-tRNA metabolism involved in translational fidelity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0002196	P		Seeded From UniProt	complete
involved_in	GO:0106074	aminoacyl-tRNA metabolism involved in translational fidelity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0002196	P		Seeded From UniProt	complete
involved_in	GO:0106074	aminoacyl-tRNA metabolism involved in translational fidelity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0002161	P		Seeded From UniProt	complete
involved_in	GO:0106074	aminoacyl-tRNA metabolism involved in translational fidelity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0002161	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002318 InterPro:IPR018162 InterPro:IPR018163 InterPro:IPR018164	F		Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003156 InterPro:IPR018165	F		Seeded From UniProt	complete
enables	GO:0004812	aminoacyl-tRNA ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012947	F		Seeded From UniProt	complete
enables	GO:0004813	alanine-tRNA ligase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018162 InterPro:IPR018164 InterPro:IPR018165 InterPro:IPR023033	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012947 InterPro:IPR018162 InterPro:IPR018164 InterPro:IPR018165	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002318 InterPro:IPR018162	C		Seeded From UniProt	complete
involved_in	GO:0006419	alanyl-tRNA aminoacylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR018162 InterPro:IPR018164 InterPro:IPR018165	P		Seeded From UniProt	complete
involved_in	GO:0043039	tRNA aminoacylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012947	P		Seeded From UniProt	complete
enables	GO:0004813	alanine-tRNA ligase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:6.1.1.7	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000023192	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000023192	F		Seeded From UniProt	complete
enables	GO:0004813	alanine-tRNA ligase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000023192	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000023192	F		Seeded From UniProt	complete
involved_in	GO:0006419	alanyl-tRNA aminoacylation	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000023192	P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
enables	GO:0004812	aminoacyl-tRNA ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0030	F		Seeded From UniProt	complete
involved_in	GO:0006412	translation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0648	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0820	F		Seeded From UniProt	complete
enables	GO:0016874	ligase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0436	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Brey, RN & Rosen, BP (1979) Properties of Escherichia coli mutants altered in calcium/proton antiport activity. J. Bacteriol. 139 824-34 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
↑ Beebe, K et al. (2003) Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 22 668-75 PubMed GONUTS page
↑ ^4.0 ^4.1 Beebe, K et al. (2008) Distinct domains of tRNA synthetase recognize the same base pair. Nature 451 90-3 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^6.0 ^6.1 Putney, SD & Schimmel, P (1981) An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription. Nature 291 632-5 PubMed GONUTS page
↑ Miller, WT et al. (1991) Evidence for a "cysteine-histidine box" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase. Biochemistry 30 6970-6 PubMed GONUTS page
↑ ^8.0 ^8.1 Putney, SD et al. (1981) Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits. J. Biol. Chem. 256 198-204 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page
↑ Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page
↑ Tsui, WC & Fersht, AR (1981) Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli. Nucleic Acids Res. 9 4627-37 PubMed GONUTS page

[PMID:383694-1] Brey, RN & Rosen, BP (1979) Properties of Escherichia coli mutants altered in calcium/proton antiport activity. J. Bacteriol. 139 824-34 PubMed GONUTS page

[PMID:16858726-2] 2.0 ^2.1 ^2.2 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page

[PMID:12554667-3] Beebe, K et al. (2003) Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability. EMBO J. 22 668-75 PubMed GONUTS page

[PMID:18172502-4] 4.0 ^4.1 Beebe, K et al. (2008) Distinct domains of tRNA synthetase recognize the same base pair. Nature 451 90-3 PubMed GONUTS page

[PMID:21873635-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:6264314-6] 6.0 ^6.1 Putney, SD & Schimmel, P (1981) An aminoacyl tRNA synthetase binds to a specific DNA sequence and regulates its gene transcription. Nature 291 632-5 PubMed GONUTS page

[PMID:1712632-7] Miller, WT et al. (1991) Evidence for a "cysteine-histidine box" metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase. Biochemistry 30 6970-6 PubMed GONUTS page

[PMID:7005211-8] 8.0 ^8.1 Putney, SD et al. (1981) Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits. J. Biol. Chem. 256 198-204 PubMed GONUTS page

[PMID:18304323-9] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:15911532-10] Lopez-Campistrous, A et al. (2005) Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell Proteomics 4 1205-9 PubMed GONUTS page

[PMID:6117825-11] Tsui, WC & Fersht, AR (1981) Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli. Nucleic Acids Res. 9 4627-37 PubMed GONUTS page

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ECOLI:SYA

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