GYRA_RICCN
ID GYRA_RICCN Reviewed; 905 AA.
AC Q92IZ6;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=RC0273;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL02811.1; -; Genomic_DNA.
DR PIR; A97734; A97734.
DR RefSeq; WP_010976933.1; NC_003103.1.
DR AlphaFoldDB; Q92IZ6; -.
DR SMR; Q92IZ6; -.
DR EnsemblBacteria; AAL02811; AAL02811; RC0273.
DR KEGG; rco:RC0273; -.
DR PATRIC; fig|272944.4.peg.310; -.
DR HOGENOM; CLU_002977_6_1_5; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000000816; 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_0000145246"
FT REGION 885..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 886..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; 100701 MW; CBB5543B3772DA53 CRC64;
MTDKSSSNLV PVNIEDEMKV SYLDYAMSVI VSRAIPDVRD GLKPVHRRII YSMHEAGNHA
SKPYRKSARI VGDVMGKYHP HGDSAIYDAL VRMAQDFSLR LPLVDGQGNF GSMDGDAAAA
MRYTESRMAK VSYKLVEDID KETVSFNPNY DGSEEEPSVL PAMFPNLLVN GSGGIAVGMA
TNIPPHNLGE VIDACCLYID NNDIEILDLL EVVKGPDFPT GSMILGISGI RSAYLTGRGS
IIMRGRAEIE NIGNNRQAII ITEIPYMVNK ARLVEKIAEM VKEKRIEGIS DLRDESNKNG
VRIFIELKKD VVAEVVLNQI YACTQLQTSF GVIMLALKDG LPKVMNLKEV IAAFVSFREV
VITNRTIYLL NKARDRAHIL LGLTIAVSNI DEIIRIIKAS NDSNAAKQEL MARQWEALNI
LPLVKLVDDK AMLNEQGKCN FTEVQAKAIL EMRLQRLTAM EKNKLEEDLK NLITEITEYL
NILGSRTRLL EILKEELIKV KEEFATPRLT SIEFGEFDQD IEDLIQREEM VVTVTLGGYI
KRVPLSSYRA QKRGGKGRSG LSMRDEDITT QVFVGSTHTP MLFFSNIGQV YSLKLYKLPL
SNPQGKGRPM VNILPLKANE HITNIMPLPE NQDERDNLNI MFATAKGNIR RSDLLDFKKL
QSNGKIAIRL DEDDKLIDVK PCKEDEHILL ATKAGKALRF PVESLRVIKS RTSDGVRGMK
LAKEDSVISM TVLKGISSTK EDRDAYLSVP WEQRLEIAKG EAFNPEELGV SLTAPAIVEM
ANSEEFILTV TENGFGKRSS AYGYRITDRG GSGIINMDIN DKTGLVVGVM PVKMDDELML
ITNSGKLIRC KLESVRITGR NTSGVILFKL DDGEKVVSVS LIAETAESEE DSELEEEGLE
QSEEV
