GYRA_RICBR
ID GYRA_RICBR Reviewed; 905 AA.
AC Q1RID9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=RBE_0794;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01897};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; CP000087; ABE04875.1; -; Genomic_DNA.
DR RefSeq; WP_011477462.1; NC_007940.1.
DR AlphaFoldDB; Q1RID9; -.
DR SMR; Q1RID9; -.
DR STRING; 336407.RBE_0794; -.
DR PRIDE; Q1RID9; -.
DR EnsemblBacteria; ABE04875; ABE04875; RBE_0794.
DR KEGG; rbe:RBE_0794; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_5; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000001951; Chromosome.
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:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR HAMAP; MF_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Topoisomerase.
FT CHAIN 1..905
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000273107"
FT REGION 882..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 551..557
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 885..905
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 905 AA; 100679 MW; 6FE9AB2C57BCCC1D CRC64;
MTDNNSSNLV PVNIEDEMKV SYLDYAMSVI VSRAIPDVRD GLKPVHRRII YSMHEAGNHA
NRAYRKSARI VGDVMGKYHP HGDSAIYDSL VRMAQDFSLR LPLVDGQGNF GSLDGDAAAA
MRYTESRMAK VAHKLIEDID KETVSFNPNY DGSEEEPSVL PSMFPNLLVN GSGGIAVGMA
TNIPPHNLGE VIDACCLYVD NNDIEILDLL EVVKGPDFPT SGIILGVNGI KSAYLTGRGS
IAIRGRAEIE NLGNGRQAII ITEIPYMVNK ARLVEKIAEM VKEKRIEGIS DLRDESNKNG
IRIYIELKKD IVAEVVLNQI YSCTQLQTSF GVIMLALKDG LPKVMNLKEV IAAFVSFREV
VITNRTIYLL NKARDKAHIL LGLTIAVSNI DEIIRIIKAA SDPNAAKQEL MARSWDALNI
LPLVKLVDDK AMLNEEGKCS FTEAQAKAIL EMRLQRLTAM EKNKLEEDLK NLATEITEYL
NILGSRERLL EILKEELIKV KEEFATPRLT SIEFGEFDQD IEDLIQREEM VVTVTLGGYI
KRVPLSSYRA QKRGGKGRSG LSMRDEDITT QVFVGSTHTP MLFFSNIGQV YSLKLYKLPL
SNPQGKGRPM VNILPLKGDE HITNIMPLPE NQDEWDNLNI MFATAKGNIR RSDLLDFKKI
QSNGKIAIRL DEDDKLIDVK PCKEDEHILL ATKSGKALRF PVESLRVIKS RTSDGVRGMR
LAEDDSVISM TVLKGIKATR EERDAYLSVS WEKRLEIAKG EEFNSEELGV DLTAESILEM
ANSEEFILTV TENGFGKRSS AYGYRITDRG GSGIINMDIN DKTGLVVGVM PVKMDDELML
ITNSGKLIRC KLETVRITGR NTSGVTLFRL DDGEKVVSAS LIAESSDDNE EDSEFEEEVA
EEGSE
