CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002955
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Translation initiation factor IF-2 
Protein Synonyms/Alias
  
Gene Name
 infB 
Gene Synonyms/Alias
 ssyG; b3168; JW3137 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
7*MTDVTIKTLAAERQacetylation[1]
42DSVSAQEKQTLIDHLacetylation[1]
52LIDHLNQKNSGPDKLacetylation[1]
58QKNSGPDKLTLQRKTacetylation[1]
93RKKRTFVKRDPQEAEacetylation[1]
125REAEESAKREAQQKAacetylation[1]
141REAAEQAKREAAEQAacetylation[1]
155AKREAAEKDKVSNQQacetylation[1]
157REAAEKDKVSNQQDDacetylation[1]
167NQQDDMTKNAQAEKAacetylation[1]
173TKNAQAEKARREQEAacetylation[1]
184EQEAAELKRKAEEEAacetylation[1]
214RRMAEENKWTDNAEPacetylation[1]
301SLQQGFQKPAQAVNRacetylation[1, 2]
334VKGSQVIKAMMKLGAacetylation[1]
502VAVNKIDKPEADPDRacetylation[1]
562LELKAVRKGMASGAVacetylation[1]
576VIESFLDKGRGPVATacetylation[1]
593VREGTLHKGDIVLCGacetylation[1]
648VTVVRDEKKAREVALacetylation[1]
710AISDSLLKLSTDEVKacetylation[1]
717KLSTDEVKVKIIGSGacetylation[1]
756RADASARKVIEAESLacetylation[1]
791GMLSPELKQQIIGLAacetylation[1]
805AEVRDVFKSPKFGAIacetylation[1]
808RDVFKSPKFGAIAGCacetylation[1, 3]
849LESLRRFKDDVNEVRacetylation[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] 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]
 [3] 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] 
Functional Description
 One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. 
Sequence Annotation
 NP_BIND 398 405 GTP (By similarity).
 NP_BIND 444 448 GTP (By similarity).
 NP_BIND 498 501 GTP (By similarity).
 REGION 1 103 1.
 REGION 104 287 2.
 REGION 288 391 3.
 REGION 392 540 G-domain.
 REGION 541 668 5.
 REGION 669 890 6.
 MOD_RES 808 808 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative initiation; Complete proteome; Cytoplasm; Direct protein sequencing; GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 890 AA 
Protein Sequence
MTDVTIKTLA AERQTSVERL VQQFADAGIR KSADDSVSAQ EKQTLIDHLN QKNSGPDKLT 60
LQRKTRSTLN IPGTGGKSKS VQIEVRKKRT FVKRDPQEAE RLAAEEQAQR EAEEQARREA 120
EESAKREAQQ KAEREAAEQA KREAAEQAKR EAAEKDKVSN QQDDMTKNAQ AEKARREQEA 180
AELKRKAEEE ARRKLEEEAR RVAEEARRMA EENKWTDNAE PTEDSSDYHV TTSQHARQAE 240
DESDREVEGG RGRGRNAKAA RPKKGNKHAE SKADREEARA AVRGGKGGKR KGSSLQQGFQ 300
KPAQAVNRDV VIGETITVGE LANKMAVKGS QVIKAMMKLG AMATINQVID QETAQLVAEE 360
MGHKVILRRE NELEEAVMSD RDTGAAAEPR APVVTIMGHV DHGKTSLLDY IRSTKVASGE 420
AGGITQHIGA YHVETENGMI TFLDTPGHAA FTSMRARGAQ ATDIVVLVVA ADDGVMPQTI 480
EAIQHAKAAQ VPVVVAVNKI DKPEADPDRV KNELSQYGIL PEEWGGESQF VHVSAKAGTG 540
IDELLDAILL QAEVLELKAV RKGMASGAVI ESFLDKGRGP VATVLVREGT LHKGDIVLCG 600
FEYGRVRAMR NELGQEVLEA GPSIPVEILG LSGVPAAGDE VTVVRDEKKA REVALYRQGK 660
FREVKLARQQ KSKLENMFAN MTEGEVHEVN IVLKADVQGS VEAISDSLLK LSTDEVKVKI 720
IGSGVGGITE TDATLAAASN AILVGFNVRA DASARKVIEA ESLDLRYYSV IYNLIDEVKA 780
AMSGMLSPEL KQQIIGLAEV RDVFKSPKFG AIAGCMVTEG VVKRHNPIRV LRDNVVIYEG 840
ELESLRRFKD DVNEVRNGME CGIGVKNYND VRTGDVIEVF EIIEIQRTIA 890 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
 GO:0003924; F:GTPase activity; IDA:EcoCyc.
 GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
 GO:0043024; F:ribosomal small subunit binding; IDA:EcoCyc.
 GO:0003743; F:translation initiation factor activity; IDA:EcoCyc. 
Interpro
 IPR009061; DNA-bd_dom_put.
 IPR000795; EF_GTP-bd_dom.
 IPR013575; IF2_assoc_dom_bac.
 IPR006847; IF2_N.
 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR000178; TF_IF2_bacterial-like.
 IPR015760; TIF_IF2.
 IPR023115; TIF_IF2_dom3.
 IPR004161; Transl_elong_EFTu/EF1A_2.
 IPR009000; Transl_elong_init/rib_B-barrel. 
Pfam
 PF00009; GTP_EFTU
 PF03144; GTP_EFTU_D2
 PF11987; IF-2
 PF08364; IF2_assoc
 PF04760; IF2_N 
SMART
  
PROSITE
 PS01176; IF2 
PRINTS