CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003538
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription termination/antitermination protein NusA 
Protein Synonyms/Alias
 N utilization substance protein A; Transcription termination/antitermination L factor 
Gene Name
 nusA 
Gene Synonyms/Alias
 b3169; JW3138 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
3*****MNKEILAVVEacetylation[1]
16VEAVSNEKALPREKIacetylation[1]
22EKALPREKIFEALESacetylation[1, 2]
36SALATATKKKYEQEIacetylation[1]
37ALATATKKKYEQEIDacetylation[1]
38LATATKKKYEQEIDVacetylation[1]
73DEVTQPTKEITLEAAacetylation[1]
111RITTQTAKQVIVQKVacetylation[1]
117AKQVIVQKVREAERAacetylation[1]
143EIITGVVKKVNRDNIacetylation[1]
224GEEVIEIKAAARDPGacetylation[1]
243IAVKTNDKRIDPVGAacetylation[1]
429EESLGDNKPADDLLNacetylation[1]
447VDRDLAFKLAARGVCacetylation[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] 
Functional Description
 Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription. 
Sequence Annotation
 DOMAIN 135 200 S1 motif.
 DOMAIN 230 293 KH 1.
 DOMAIN 302 368 KH 2.
 REPEAT 364 414 1.
 REPEAT 439 489 2.
 REGION 364 489 2 X 51 AA approximate repeats.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Reference proteome; Repeat; RNA-binding; Stress response; Transcription; Transcription antitermination; Transcription regulation; Transcription termination. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 495 AA 
Protein Sequence
MNKEILAVVE AVSNEKALPR EKIFEALESA LATATKKKYE QEIDVRVQID RKSGDFDTFR 60
RWLVVDEVTQ PTKEITLEAA RYEDESLNLG DYVEDQIESV TFDRITTQTA KQVIVQKVRE 120
AERAMVVDQF REHEGEIITG VVKKVNRDNI SLDLGNNAEA VILREDMLPR ENFRPGDRVR 180
GVLYSVRPEA RGAQLFVTRS KPEMLIELFR IEVPEIGEEV IEIKAAARDP GSRAKIAVKT 240
NDKRIDPVGA CVGMRGARVQ AVSTELGGER IDIVLWDDNP AQFVINAMAP ADVASIVVDE 300
DKHTMDIAVE AGNLAQAIGR NGQNVRLASQ LSGWELNVMT VDDLQAKHQA EAHAAIDTFT 360
KYLDIDEDFA TVLVEEGFST LEELAYVPMK ELLEIEGLDE PTVEALRERA KNALATIAQA 420
QEESLGDNKP ADDLLNLEGV DRDLAFKLAA RGVCTLEDLA EQGIDDLADI EGLTDEKAGA 480
LIMAARNICW FGDEA 495 
Gene Ontology
 GO:0005829; C:cytosol; IDA:EcoCyc.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0006353; P:DNA-dependent transcription, termination; IEA:UniProtKB-KW.
 GO:0031564; P:transcription antitermination; IMP:EcoliWiki. 
Interpro
 IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
 IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
 IPR004087; KH_dom.
 IPR015946; KH_dom-like_a/b.
 IPR025249; KH_dom_NusA-like.
 IPR004088; KH_dom_type_1.
 IPR009019; KH_prok-type.
 IPR012340; NA-bd_OB-fold.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR022967; RNA-binding_domain_S1.
 IPR013735; TF_NusA_N.
 IPR010214; Tscrpt_termin_fac_NusA_C_rpt.
 IPR010213; Tscrpt_termination_fac_NusA. 
Pfam
 PF13184; KH_5
 PF08529; NusA_N
 PF00575; S1 
SMART
 SM00278; HhH1
 SM00322; KH
 SM00316; S1 
PROSITE
 PS50084; KH_TYPE_1
 PS50126; S1 
PRINTS