CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003490
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DNA gyrase subunit A 
Protein Synonyms/Alias
  
Gene Name
 gyrA 
Gene Synonyms/Alias
 hisW; nalA; parD; b2231; JW2225 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
61VLGNDWNKAYKKSARacetylation[1]
76VVGDVIGKYHPHGDSacetylation[1]
129YTEIRLAKIAHELMAacetylation[1]
140ELMADLEKETVDFVDacetylation[1]
154DNYDGTEKIPDVMPTacetylation[1]
253AEVEVDAKTGRETIIacetylation[1]
276NKARLIEKIAELVKEacetylation[1]
282EKIAELVKEKRVEGIacetylation[1]
308MRIVIEVKRDAVGEVacetylation[1]
348QPKIMNLKDIIAAFVacetylation[1]
407APTPAEAKTALVANPacetylation[1]
465ILDLRLQKLTGLEHEacetylation[1, 2]
473LTGLEHEKLLDEYKEacetylation[1]
516VREQFGDKRRTEITAacetylation[1]
573GKSAARIKEEDFIDRacetylation[1]
603RGRVYSMKVYQLPEAacetylation[1]
645TEFEEGVKVFMATANacetylation[1, 2]
731IRLGEGDKVVSLIVPacetylation[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
 DNA gyrase negatively supercoils closed circular double- stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. 
Sequence Annotation
 ACT_SITE 122 122 O-(5'-phospho-DNA)-tyrosine intermediate.  
Keyword
 3D-structure; Antibiotic resistance; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Isomerase; Nucleotide-binding; Reference proteome; Topoisomerase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 875 AA 
Protein Sequence
MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN 60
KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM 120
RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT 180
NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV 240
YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG 300
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE 360
VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV 420
AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE 480
LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV 540
VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY 600
SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL 660
TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG 720
VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN 780
GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA 840
EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE 875 
Gene Ontology
 GO:0005694; C:chromosome; IEA:InterPro.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0009295; C:nucleoid; IBA:RefGenome.
 GO:0005524; F:ATP binding; IEA:HAMAP.
 GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IDA:EcoliWiki.
 GO:0007059; P:chromosome segregation; IBA:RefGenome.
 GO:0006265; P:DNA topological change; IMP:EcoliWiki.
 GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
 GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
 GO:0042493; P:response to drug; IMP:EcoliWiki.
 GO:0006351; P:transcription, DNA-dependent; IDA:EcoliWiki. 
Interpro
 IPR024946; Arg_repress_C-like.
 IPR005743; GyrA.
 IPR006691; GyrA/parC_pinwhl.
 IPR002205; Topo_IIA_A/C.
 IPR013758; Topo_IIA_A/C_ab.
 IPR013757; Topo_IIA_A_a.
 IPR013760; Topo_IIA_like_dom. 
Pfam
 PF03989; DNA_gyraseA_C
 PF00521; DNA_topoisoIV 
SMART
 SM00434; TOP4c 
PROSITE
  
PRINTS