CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002502
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phenylalanine--tRNA ligase beta subunit 
Protein Synonyms/Alias
 Phenylalanyl-tRNA synthetase beta subunit; PheRS 
Gene Name
 pheT 
Gene Synonyms/Alias
 b1713; JW1703 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
104AVLPGDFKIKAAKLRacetylation[1]
106LPGDFKIKAAKLRGEacetylation[1]
235APTPLWMKEKLRRCGacetylation[1]
282GIVVRMAKEGETLVLacetylation[1]
296LLDGTEAKLNADTLVacetylation[1]
371VDPALQHKAMERATRacetylation[1]
441GCEVTEGKDEWQAVAacetylation[1]
496READLSLKRVKTLLNacetylation[1]
609EEHWNLAKETVDFYDacetylation[1]
630SVLDLTGKLNEVEFRacetylation[1]
655QSAAIYLKGERIGFVacetylation[1]
780EIAATVAKCVEALKEacetylation[1]
786AKCVEALKERFQASLacetylation[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] 
Functional Description
  
Sequence Annotation
 DOMAIN 39 148 tRNA-binding.
 DOMAIN 401 476 B5.
 DOMAIN 701 794 FDX-ACB.
 METAL 454 454 Magnesium (By similarity).
 METAL 460 460 Magnesium; via carbonyl oxygen (By
 METAL 463 463 Magnesium (By similarity).
 METAL 464 464 Magnesium (By similarity).  
Keyword
 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 795 AA 
Protein Sequence
MKFSELWLRE WVNPAIDSDA LANQITMAGL EVDGVEPVAG SFHGVVVGEV VECAQHPNAD 60
KLRVTKVNVG GDRLLDIVCG APNCRQGLRV AVATIGAVLP GDFKIKAAKL RGEPSEGMLC 120
SFSELGISDD HSGIIELPAD APIGTDIREY LKLDDNTIEI SVTPNRADCL GIIGVARDVA 180
VLNQLPLVQP EIVPVGATID DTLPITVEAP EACPRYLGRV VKGINVKAPT PLWMKEKLRR 240
CGIRSIDAVV DVTNYVLLEL GQPMHAFDKD RIEGGIVVRM AKEGETLVLL DGTEAKLNAD 300
TLVIADHNKA LAMGGIFGGE HSGVNDETQN VLLECAFFSP LSITGRARRH GLHTDASHRY 360
ERGVDPALQH KAMERATRLL IDICGGEAGP VIDITNEATL PKRATITLRR SKLDRLIGHH 420
IADEQVTDIL RRLGCEVTEG KDEWQAVAPS WRFDMEIEED LVEEVARVYG YNNIPDEPVQ 480
ASLIMGTHRE ADLSLKRVKT LLNDKGYQEV ITYSFVDPKV QQMIHPGVEA LLLPSPISVE 540
MSAMRLSLWT GLLATVVYNQ NRQQNRVRIF ESGLRFVPDT QAPLGIRQDL MLAGVICGNR 600
YEEHWNLAKE TVDFYDLKGD LESVLDLTGK LNEVEFRAEA NPALHPGQSA AIYLKGERIG 660
FVGVVHPELE RKLDLNGRTL VFELEWNKLA DRVVPQAREI SRFPANRRDI AVVVAENVPA 720
ADILSECKKV GVNQVVGVNL FDVYRGKGVA EGYKSLAISL ILQDTSRTLE EEEIAATVAK 780
CVEALKERFQ ASLRD 795 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:HAMAP.
 GO:0000049; F:tRNA binding; IEA:HAMAP.
 GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:HAMAP.
 GO:0008033; P:tRNA processing; IEA:InterPro. 
Interpro
 IPR005146; B3/B4_tRNA-bd.
 IPR009061; DNA-bd_dom_put.
 IPR012340; NA-bd_OB-fold.
 IPR004532; Phe-tRNA-ligase_IIc_bsu_bac.
 IPR020825; Phe-tRNA_synthase_B3/B4.
 IPR005121; PheS_beta_Fdx_antiC-bd.
 IPR002547; tRNA-bd_dom.
 IPR005147; tRNA_synthase_B5-dom. 
Pfam
 PF03483; B3_4
 PF03484; B5
 PF03147; FDX-ACB
 PF01588; tRNA_bind 
SMART
 SM00873; B3_4
 SM00874; B5
 SM00896; FDX-ACB 
PROSITE
 PS51483; B5
 PS51447; FDX_ACB
 PS50886; TRBD 
PRINTS