ID A1AD84_ECOK1 Unreviewed; 875 AA.
AC A1AD84;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=DNA gyrase subunit A;
DE EC=5.99.1.3;
GN Name=gyrA; OrderedLocusNames=Ecok1_21300; ORFNames=APECO1_4329;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/JB.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain
RT O1:K1:H7 shares strong similarities with human extraintestinal
RT pathogenic E. coli genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC stranded DNA in an ATP-dependent manner and also catalyzes the
CC interconversion of other topological isomers of double-stranded
CC DNA rings, including catenanes and knotted rings (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC of double-stranded DNA.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC Within the heterotetramer, GyrA contains the active site tyrosine
CC that forms a covalent intermediate with the DNA, while GyrB
CC contributes the cofactor binding sites and catalyzes ATP
CC hydrolysis (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the topoisomerase GyrA/ParC subunit family.
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DR EMBL; CP000468; ABJ01624.1; -; Genomic_DNA.
DR RefSeq; YP_853338.1; NC_008563.1.
DR ProteinModelPortal; A1AD84; -.
DR SMR; A1AD84; 30-522, 535-841.
DR STRING; 405955.APECO1_4329; -.
DR EnsemblBacteria; ABJ01624; ABJ01624; APECO1_4329.
DR GeneID; 4492577; -.
DR KEGG; ecv:APECO1_4329; -.
DR PATRIC; 18216383; VBIEscCol127180_2453.
DR eggNOG; COG0188; -.
DR HOGENOM; HOG000076278; -.
DR KO; K02469; -.
DR OMA; IAQEDVV; -.
DR ProtClustDB; PRK05560; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR HAMAP; MF_01897; GyrA; 1; -.
DR InterPro; IPR024946; Arg_repress_C-like.
DR InterPro; IPR005743; GyrA.
DR InterPro; IPR006691; GyrA/parC_pinwhl.
DR InterPro; IPR002205; Topo_IIA_A/C.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a.
DR InterPro; IPR013760; Topo_IIA_like_dom.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR TIGRFAMs; TIGR01063; gyrA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Topoisomerase.
FT ACT_SITE 122 122 O-(5'-phospho-DNA)-tyrosine intermediate
FT (By similarity).
SQ SEQUENCE 875 AA; 96994 MW; 507E4D87A4D364CE CRC64;
MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE
VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV
AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV
VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY
SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL
TEFNRLRTAG KVAIKLVEGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG
VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN
GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTSED ENVVGLQRVA
EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE
//
