GYRA_RICTY
ID GYRA_RICTY Reviewed; 905 AA.
AC Q68XG2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=RT0196;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03680.1; -; Genomic_DNA.
DR RefSeq; WP_011190667.1; NC_006142.1.
DR AlphaFoldDB; Q68XG2; -.
DR SMR; Q68XG2; -.
DR STRING; 257363.RT0196; -.
DR EnsemblBacteria; AAU03680; AAU03680; RT0196.
DR KEGG; rty:RT0196; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_5; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000604; 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_0000273109"
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 905 AA; 101155 MW; C5ABFD3BED0BF325 CRC64;
MTDKYSSNLV PVNIEDEMKA SYLDYAMSVI VSRAIPDVRD GLKPVHRRII YSMYEAGNHA
SKPYRKSARI VGDVMGKYHP HGDSAIYDSL VRMTQDFSLR LPLVDGQGNF GSMDGDAAAA
MRYTESRMSK VAHKLVEDID KGTVSFNINY DGSEEEPSVL PAMFPNLLVN GSGGIAVGMA
TNIPPHNLGE IIDACCLYID NNDIEILDLL EVVKGPDFPT GSMILGISGI RSAYLTGRGS
IIMRGKAEIE NIGNSRQAII ITEIPYMVNK ARLVEKIAEM VKEKRIEGIS DLRDESNKNG
VRIFIELKKD VVAEVVLNQI YACTQLQTNF GVIMLALKDG LPKVMNLKEV IAAFVSFREV
VITNRTIYLL NKARDRAHIL LGLAIAISNI DEIIYIIKAS NDTNLAKQEL MDRQWEVLDI
LPLIKLVDDK VMLNERGKLS FTEVQAKAIL EMKLQRLTAM EKNKLEQDLK HLATEIAEYL
NILDSRTRLL EILKEELIKV KEEFAVPRLT AIEFGEFDQD IEDLIQREEM VVTVTLGGYI
KRVPLSSYRS QKRGGKGRSG LSMRDEDITM QVFVGSTHTP MLFFSNIGKV YSLKLYKLPL
SNPQGKGRPM VNILPLQENE HITNIMPLPE NQDEWDHLNI MFATAKGNIR RSDLLDFKKI
QLNGKIAIRL DEDDKLIDVK PCKEDEHILL ATKAGKALRF PVESLRIIKS RISDGVRGMK
LAKEDSVISM TVLKGINSTK EDRDAYLTVP WEKRLKIAKG EEFNLEALGV HLNADSILEM
ANSEEFILTV TENGFGKRSS AYGYRITDRG GSGIINMDIN DKTGLVVGVM PVKMDDELML
ITNSGKLIRC KLESVRITGR NTSGVILFKL DDDEKVVSVS LIAETSESGE DSELVEDGLE
SAENM
