GYRA_RICFE
ID GYRA_RICFE Reviewed; 906 AA.
AC Q4UKM1;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, 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=RF_1055;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61906.1; -; Genomic_DNA.
DR RefSeq; WP_011271367.1; NC_007109.1.
DR AlphaFoldDB; Q4UKM1; -.
DR SMR; Q4UKM1; -.
DR STRING; 315456.RF_1055; -.
DR EnsemblBacteria; AAY61906; AAY61906; RF_1055.
DR KEGG; rfe:RF_1055; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_5; -.
DR OMA; EIDANKH; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000008548; 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..906
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000273108"
FT REGION 886..906
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 ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 906 AA; 101121 MW; 20FE68CE7B0F8FB0 CRC64;
MTDQNFSNLV PVNIEDEMKV SYLDYAMSVI VSRAIPDVRD GLKPVHRRII YSMYEAGNHA
SKPYRKSARI VGDVMGKYHP HGDSAIYDSL VRMAQDFSLR LPLVDGQGNF GSMDGDAAAA
MRYTESRMAK VSHKLVEDID KETVSFNPNY DGSEEEPSVL PAMFPNLLVN GSGGIAVGMA
TNIPPHNLGE VIDACCLYID NNDIEILDLL EVVKGPDFPT GSMILGISGI RSAYLTGRGS
IIMRGRAEIE NIGNSRQAII ITEIPYMVNK ARLVEKIAEM VKEKRIEGIS DLRDESNKNG
VRIFIELKKD VVVEVVLNQI YACTQLQTSF GVIMLALKDG LPKVMNLKEV IAAFVSFREV
VITNRTIYLL NKARDRAHIL LGLTIAVSNI DEIIRIIKAS NNPNAAKQEL MARSWDALNI
LPLVKLVDDK AMLNEQGKCS FTEVQAKAIL EMRLQRLTAM EKNKLEEDLK NLATEITEYL
NILGSRTRLL EILKEELIKV KEEFATPRLT SIEFGEFDQD IEDLIQREEM VVTVTLGGYI
KRVPLSSYRA QKRGGKGRSG LSMRDEDITT QVFVGSTHTP MLFFSNIGQV YSLKLYKLPL
SNPQGKGRPM VNILPLKENE HITNIMPLPE NQDEWDNLNI MFATAKGNIR RSDLLDFKKI
QSNGKIAIRL DEDDKLIDVK PCKEDEHILL ATKAGKALRF PVESLRVIKS RTSDGVRGMK
LAKEDSVISM TVLKGISSTK EDRDAYLTVP WEKRLEIAKG EEFNLEELGV TLTADSILEM
ANSEEFILTV TENGFGKRSS AYGYRITDRG GSGIINMDIN DKTGLVVGVM PVKMDDELML
ITNSGKLIRC KLESVRITGR NTSGVILFKL DDGEKVVSVS LIAETSESEE DSELEEDLEQ
AEEVYT
