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Protein

Alanine--tRNA ligase

Gene

alaS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). AlaRS also incorrectly activates the sterically smaller than alanine amino acid glycine as well as the sterically larger amino acid serine. These incorrectly charged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (glycine and serine) in the charging step.
Edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr).
Attaches Ala to transfer-messenger RNA (tmRNA, also known as 10Sa RNA, the product of the ssrA gene). tmRNA plays a major role in rescue of stalled ribosomes via trans-translation.1 Publication

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit; it is not clear where this binding occurs.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi564 – 5641ZincBy similarity
Metal bindingi568 – 5681ZincBy similarity
Metal bindingi666 – 6661ZincBy similarity
Metal bindingi670 – 6701ZincBy similarity

GO - Molecular functioni

  • alanine-tRNA ligase activity Source: EcoCyc
  • amino acid binding Source: GO_Central
  • aminoacyl-tRNA editing activity Source: UniProtKB
  • ATP binding Source: UniProtKB-HAMAP
  • identical protein binding Source: IntAct
  • transcriptional repressor activity, bacterial-type RNA polymerase core promoter proximal region sequence-specific binding Source: EcoCyc
  • tRNA binding Source: GO_Central
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • alanyl-tRNA aminoacylation Source: EcoCyc
  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • regulation of translational fidelity Source: GOC
  • tRNA modification Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:ALAS-MONOMER.
ECOL316407:JW2667-MONOMER.
MetaCyc:ALAS-MONOMER.
BRENDAi6.1.1.7. 2026.

Protein family/group databases

MoonProtiP00957.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Gene namesi
Name:alaS
Synonyms:lovB
Ordered Locus Names:b2697, JW2667
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10034. alaS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi179 – 1791C → S: Inactivates the enzyme. 1 Publication
Mutagenesisi182 – 1821C → S: No inactivation. 1 Publication
Mutagenesisi184 – 1841E → Q: No inactivation. 1 Publication
Mutagenesisi188 – 1881D → N: No inactivation. 1 Publication
Mutagenesisi189 – 1891H → Q: Inactivates the enzyme. 1 Publication
Mutagenesisi191 – 1911D → N: No inactivation. 1 Publication
Mutagenesisi192 – 1921H → Q: Inactivates the enzyme. 1 Publication
Mutagenesisi236 – 2361D → A or N: Decreases affinity for alanine without improving discrimination against serine. 1 Publication
Mutagenesisi238 – 2381G → A: Greatly decreases affinity for alanine with only small changes in affinity for serine and glycine, in a 2-442 residue construct. 1 Publication
Mutagenesisi564 – 5641H → A: No effect on tRNA editing. 1 Publication
Mutagenesisi568 – 5681H → A: No effect on tRNA editing. 1 Publication
Mutagenesisi584 – 5841Q → H: Loss of mischarged tRNA editing activity; when associated with A-666. 2 Publications
Mutagenesisi666 – 6661C → A: Loss of mischarged tRNA editing activity; when associated with H-584 the effect is more pronounced. 2 Publications
Mutagenesisi670 – 6701H → A: No effect on tRNA editing. 1 Publication
Mutagenesisi693 – 6931R → K: Reduces specificity of editing activity for tRNA(Ala), allows editing of tRNA(Thr). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 876875Alanine--tRNA ligasePRO_0000075113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP00957.
PaxDbiP00957.
PRIDEiP00957.

2D gel databases

SWISS-2DPAGEP00957.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-544061,EBI-544061

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi851507. 1 interaction.
DIPiDIP-9080N.
IntActiP00957. 19 interactions.
MINTiMINT-1266342.
STRINGi511145.b2697.

Structurei

Secondary structure

1
876
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 1814Combined sources
Helixi43 – 475Combined sources
Helixi48 – 514Combined sources
Beta strandi60 – 6910Combined sources
Helixi78 – 803Combined sources
Turni81 – 833Combined sources
Beta strandi84 – 863Combined sources
Beta strandi89 – 10113Combined sources
Helixi104 – 11613Combined sources
Turni118 – 1214Combined sources
Helixi125 – 1273Combined sources
Beta strandi128 – 1336Combined sources
Helixi137 – 1459Combined sources
Helixi151 – 1533Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi170 – 18819Combined sources
Turni201 – 2044Combined sources
Beta strandi205 – 22117Combined sources
Beta strandi223 – 2253Combined sources
Beta strandi227 – 24014Combined sources
Helixi241 – 2488Combined sources
Helixi254 – 2563Combined sources
Helixi258 – 27114Combined sources
Helixi279 – 29618Combined sources
Helixi305 – 32420Combined sources
Helixi331 – 3344Combined sources
Helixi335 – 3428Combined sources
Helixi343 – 3464Combined sources
Helixi347 – 3515Combined sources
Helixi353 – 36816Combined sources
Helixi371 – 38313Combined sources
Beta strandi387 – 3904Combined sources
Helixi392 – 40211Combined sources
Helixi406 – 4149Combined sources
Turni415 – 4173Combined sources
Helixi422 – 44019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HXUX-ray2.10A2-442[»]
3HXVX-ray1.93A2-442[»]
3HXWX-ray1.93A2-442[»]
3HXXX-ray2.11A2-442[»]
3HXYX-ray2.27A2-442[»]
3HXZX-ray1.99A/B/C/D2-442[»]
3HY0X-ray1.90A/B2-442[»]
3HY1X-ray2.79A/B2-442[»]
ProteinModelPortaliP00957.
SMRiP00957. Positions 2-873.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00957.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 461460CatalyticAdd
BLAST
Regioni553 – 705153EditingAdd
BLAST
Regioni699 – 808110Important for oligomerizationAdd
BLAST
Regioni766 – 875110C-Ala domainAdd
BLAST

Domaini

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.
The editing domain removes incorrectly charged amino acids, i.e. Ser-tRNA(Ala) or Gly-tRNA(Ala) become uncharged tRNA(Ala) and the amino acid. It is specific for the acceptor stem of tRNA(Ala).
The C-terminal 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. This C-Ala domain can be replaced in vitro by the corresponding domain of Aquifex aeolicus or man. Recognition of tRNA(Ala) by the 2 domains is independent, that is one enzyme recognizes the same tRNA(Ala) in 2 different manners.Curated

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105CIM. Bacteria.
COG0013. LUCA.
HOGENOMiHOG000156964.
InParanoidiP00957.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG6Q2SQ2.
PhylomeDBiP00957.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00957-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV
60 70 80 90 100
FLGLDKRNYS RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG
110 120 130 140 150
DYFKHDAIQF AWELLTSEKW FALPKERLWV TVYESDDEAY EIWEKEVGIP
160 170 180 190 200
RERIIRIGDN KGAPYASDNF WQMGDTGPCG PCTEIFYDHG DHIWGGPPGS
210 220 230 240 250
PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG LERIAAVLQH
260 270 280 290 300
VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM
310 320 330 340 350
PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK
360 370 380 390 400
RQQAQVEQVL KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD
410 420 430 440 450
TYGFPVDLTA DVCRERNIKV DEAGFEAAME EQRRRAREAS GFGADYNAMI
460 470 480 490 500
RVDSASEFKG YDHLELNGKV TALFVDGKAV DAINAGQEAV VVLDQTPFYA
510 520 530 540 550
ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG SLKVGDAVQA
560 570 580 590 600
DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH
610 620 630 640 650
NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD
660 670 680 690 700
ERVRVLSMGD FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG
710 720 730 740 750
EGAIATVHAD SDRLSEVAHL LKGDSNNLAD KVRSVLERTR QLEKELQQLK
760 770 780 790 800
EQAAAQESAN LSSKAIDVNG VKLLVSELSG VEPKMLRTMV DDLKNQLGST
810 820 830 840 850
IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG GKGGGRPDMA
860 870
QAGGTDAAAL PAALASVKGW VSAKLQ
Length:876
Mass (Da):96,032
Last modified:November 1, 1997 - v2
Checksum:i73F69C69FCF8C08C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 335LVPHN → RYPIT (PubMed:7005898).Curated
Sequence conflicti29 – 335LVPHN → RYPIT in AAA03208 (PubMed:7025207).Curated
Sequence conflicti158 – 1581G → N (PubMed:7005898).Curated
Sequence conflicti158 – 1581G → N in AAA03208 (PubMed:7025207).Curated
Sequence conflicti168 – 1681D → G in AAA03208 (PubMed:7025207).Curated
Sequence conflicti172 – 1721Q → R in AAA03208 (PubMed:7025207).Curated
Sequence conflicti175 – 1751D → G in AAA03208 (PubMed:7025207).Curated
Sequence conflicti180 – 1801G → D in AAA03208 (PubMed:7025207).Curated
Sequence conflicti584 – 5841Q → H in AAA03208 (PubMed:7025207).Curated
Sequence conflicti619 – 6191Q → L in AAA03208 (PubMed:7025207).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75739.1.
AP009048 Genomic DNA. Translation: BAA16559.1.
J01581 Unassigned DNA. Translation: AAA03208.1.
L07596 Unassigned DNA. Translation: AAA71918.1. Sequence problems.
D44453 Genomic DNA. Translation: BAA21554.1.
Z28405 Genomic DNA. Translation: CAA82247.1.
PIRiE65049. SYECAT.
RefSeqiNP_417177.1. NC_000913.3.
WP_000047184.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75739; AAC75739; b2697.
BAA16559; BAA16559; BAA16559.
GeneIDi947175.
KEGGiecj:JW2667.
eco:b2697.
PATRICi32120790. VBIEscCol129921_2787.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC75739.1.
AP009048 Genomic DNA. Translation: BAA16559.1.
J01581 Unassigned DNA. Translation: AAA03208.1.
L07596 Unassigned DNA. Translation: AAA71918.1. Sequence problems.
D44453 Genomic DNA. Translation: BAA21554.1.
Z28405 Genomic DNA. Translation: CAA82247.1.
PIRiE65049. SYECAT.
RefSeqiNP_417177.1. NC_000913.3.
WP_000047184.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HXUX-ray2.10A2-442[»]
3HXVX-ray1.93A2-442[»]
3HXWX-ray1.93A2-442[»]
3HXXX-ray2.11A2-442[»]
3HXYX-ray2.27A2-442[»]
3HXZX-ray1.99A/B/C/D2-442[»]
3HY0X-ray1.90A/B2-442[»]
3HY1X-ray2.79A/B2-442[»]
ProteinModelPortaliP00957.
SMRiP00957. Positions 2-873.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi851507. 1 interaction.
DIPiDIP-9080N.
IntActiP00957. 19 interactions.
MINTiMINT-1266342.
STRINGi511145.b2697.

Protein family/group databases

MoonProtiP00957.

2D gel databases

SWISS-2DPAGEP00957.

Proteomic databases

EPDiP00957.
PaxDbiP00957.
PRIDEiP00957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75739; AAC75739; b2697.
BAA16559; BAA16559; BAA16559.
GeneIDi947175.
KEGGiecj:JW2667.
eco:b2697.
PATRICi32120790. VBIEscCol129921_2787.

Organism-specific databases

EchoBASEiEB0033.
EcoGeneiEG10034. alaS.

Phylogenomic databases

eggNOGiENOG4105CIM. Bacteria.
COG0013. LUCA.
HOGENOMiHOG000156964.
InParanoidiP00957.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG6Q2SQ2.
PhylomeDBiP00957.

Enzyme and pathway databases

BioCyciEcoCyc:ALAS-MONOMER.
ECOL316407:JW2667-MONOMER.
MetaCyc:ALAS-MONOMER.
BRENDAi6.1.1.7. 2026.

Miscellaneous databases

EvolutionaryTraceiP00957.
PROiP00957.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. Ala-tRNA-lgiase_IIc.
IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
IPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR023033. Ala_tRNA_ligase_euk/bac.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Mass spectra of partial protein hydrolysates as a multiple phase check for long polypeptides deduced from DNA sequences: NH2-terminal segment of alanine tRNA synthetase."
    Herlihy W.C., Royal N.J., Biemann K., Putney S.D., Schimmel P.R.
    Proc. Natl. Acad. Sci. U.S.A. 77:6531-6535(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166, PARTIAL PROTEIN SEQUENCE.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-876.
  6. "Purification and properties of alanine tRNA synthetase from Escherichia coli A tetramer of identical subunits."
    Putney S.D., Sauer R.T., Schimmel P.R.
    J. Biol. Chem. 256:198-204(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12, SUBUNIT.
  7. "Acceptor helix interactions in a class II tRNA synthetase: photoaffinity cross-linking of an RNA miniduplex substrate."
    Musier-Forsyth K., Schimmel P.
    Biochemistry 33:773-779(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 163-173.
  8. "Evidence for involvement of Escherichia coli genes pmbA, csrA and a previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F."
    Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T., Sekimizu K., Miki T.
    J. Mol. Biol. 256:483-502(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 799-876.
    Strain: KP4714.
  9. "Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties."
    Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.
    J. Bacteriol. 175:4744-4755(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 866-876.
    Strain: K12.
  10. "Cloning, partial sequencing, and in vitro transcription of the gene for alanine tRNA synthetase."
    Putney S.D., Melendez D.L., Schimmel P.R.
    J. Biol. Chem. 256:205-211(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
  11. "Evidence for a 'cysteine-histidine box' metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase."
    Miller W.T., Hill K.A.W., Schimmel P.
    Biochemistry 30:6970-6976(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ZINC-BINDING, MUTAGENESIS OF CYS-179; CYS-182; GLU-184; ASP-188; HIS-189; ASP-191 AND HIS-192.
  12. "A tRNA-like structure is present in 10Sa RNA, a small stable RNA from Escherichia coli."
    Komine Y., Kitabatake M., Yokogawa T., Nishikawa K., Inokuchi H.
    Proc. Natl. Acad. Sci. U.S.A. 91:9223-9227(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AMINOACYLATION OF TMRNA.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  13. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  14. "Elucidation of tRNA-dependent editing by a class II tRNA synthetase and significance for cell viability."
    Beebe K., Ribas De Pouplana L., Schimmel P.
    EMBO J. 22:668-675(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRNA EDITING, MUTAGENESIS OF HIS-564; HIS-568; GLN-584; CYS-666 AND HIS-670.
  15. "Natural homolog of tRNA synthetase editing domain rescues conditional lethality caused by mistranslation."
    Chong Y.E., Yang X.L., Schimmel P.
    J. Biol. Chem. 283:30073-30078(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRNA EDITING, MUTAGENESIS OF GLN-584 AND CYS-666.
    Strain: K12.
  16. "Distinct domains of tRNA synthetase recognize the same base pair."
    Beebe K., Mock M., Merriman E., Schimmel P.
    Nature 451:90-93(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN EDITING, MUTAGENESIS OF ARG-693.
  17. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  18. "The C-Ala domain brings together editing and aminoacylation functions on one tRNA."
    Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.
    Science 325:744-747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRNA-BINDING VIA C-ALA DOMAIN, DOMAIN EXCHANGE EXPERIMENTS.
  19. "Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma."
    Guo M., Chong Y.E., Shapiro R., Beebe K., Yang X.L., Schimmel P.
    Nature 462:808-812(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-442 WITH AND WITHOUT CHARGED CORRECT AND INCORRECT AMINO ACID, MUTAGENESIS OF ASP-236 AND GLY-238.

Entry informationi

Entry nameiSYA_ECOLI
AccessioniPrimary (citable) accession number: P00957
Secondary accession number(s): P78279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: March 16, 2016
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.