CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001849
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 alaS 
Gene Synonyms/Alias
 lovB; b2697; JW2667 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
19FLDFFHSKGHQVVASacetylation[1]
56DVFLGLDKRNYSRATacetylation[1]
74RCVRAGGKHNDLENVacetylation[1, 2]
125EKWFALPKERLWVTVacetylation[1]
232GTMEPLPKPSVDTGMacetylation[1]
269TLIQAVAKVTGATDLacetylation[1, 3]
279GATDLSNKSLRVIADacetylation[1]
327HGNMLGAKETFFYKLacetylation[1]
350GSAGEDLKRQQAQVEacetylation[1]
361AQVEQVLKTEEEQFAacetylation[1]
384LLDEELAKLSGDTLDacetylation[1]
459VDSASEFKGYDHLELacetylation[1]
478TALFVDGKAVDAINAacetylation[1]
509SGGQVGDKGELKGANacetylation[1]
526FAVEDTQKYGQAIGHacetylation[1]
536QAIGHIGKLAAGSLKacetylation[1]
585LGTHVSQKGSLVNDKacetylation[1]
592KGSLVNDKVLRFDFSacetylation[1]
605FSHNEAMKPEEIRAVacetylation[1]
637IMDLEAAKAKGAMALacetylation[1]
639DLEAAKAKGAMALFGacetylation[1]
648AMALFGEKYDERVRVacetylation[1]
722SEVAHLLKGDSNNLAacetylation[1]
731DSNNLADKVRSVLERacetylation[1]
744ERTRQLEKELQQLKEacetylation[1]
750EKELQQLKEQAAAQEacetylation[1]
764ESANLSSKAIDVNGVacetylation[1]
772AIDVNGVKLLVSELSacetylation[1]
784ELSGVEPKMLRTMVDacetylation[1, 3]
820SLIAGVSKDVTDRVKacetylation[1, 3]
827KDVTDRVKAGELIGMacetylation[1]
868PAALASVKGWVSAKLacetylation[1]
874VKGWVSAKLQ*****acetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] 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 CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [3] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 
Functional Description
 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. 
Sequence Annotation
 REGION 2 461 Catalytic.
 REGION 553 705 Editing.
 REGION 699 808 Important for oligomerization.
 REGION 766 875 C-Ala domain.
 METAL 564 564 Zinc (By similarity).
 METAL 568 568 Zinc (By similarity).
 METAL 666 666 Zinc (By similarity).
 METAL 670 670 Zinc (By similarity).
 MOD_RES 74 74 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 876 AA 
Protein Sequence
MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV FLGLDKRNYS 60
RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKHDAIQF AWELLTSEKW 120
FALPKERLWV TVYESDDEAY EIWEKEVGIP RERIIRIGDN KGAPYASDNF WQMGDTGPCG 180
PCTEIFYDHG DHIWGGPPGS PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG 240
LERIAAVLQH VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM 300
PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK RQQAQVEQVL 360
KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD TYGFPVDLTA DVCRERNIKV 420
DEAGFEAAME EQRRRAREAS GFGADYNAMI RVDSASEFKG YDHLELNGKV TALFVDGKAV 480
DAINAGQEAV VVLDQTPFYA ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG 540
SLKVGDAVQA DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH 600
NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD ERVRVLSMGD 660
FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG EGAIATVHAD SDRLSEVAHL 720
LKGDSNNLAD KVRSVLERTR QLEKELQQLK EQAAAQESAN LSSKAIDVNG VKLLVSELSG 780
VEPKMLRTMV DDLKNQLGST IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG 840
GKGGGRPDMA QAGGTDAAAL PAALASVKGW VSAKLQ 876 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0004813; F:alanine-tRNA ligase activity; IDA:EcoCyc.
 GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0001141; F:bacterial-type RNA polymerase core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IDA:EcoCyc.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IDA:EcoCyc.
 GO:0006419; P:alanyl-tRNA aminoacylation; IDA:EcoCyc. 
Interpro
 IPR002318; 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; Pesterase_DHHA1.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF02272; DHHA1
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.