GYRA_RICPR
ID GYRA_RICPR Reviewed; 905 AA.
AC P41080;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=RP206;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=7828873; DOI=10.1016/0378-1119(94)90655-6;
RA Wood D.O., Waite R.T.;
RT "Sequence analysis of the Rickettsia prowazekii gyrA gene.";
RL Gene 151:191-196(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U02931; AAA68146.1; -; Genomic_DNA.
DR EMBL; AJ235270; CAA14671.1; -; Genomic_DNA.
DR PIR; H71731; H71731.
DR RefSeq; NP_220594.1; NC_000963.1.
DR RefSeq; WP_004595986.1; NC_000963.1.
DR AlphaFoldDB; P41080; -.
DR SMR; P41080; -.
DR STRING; 272947.RP206; -.
DR EnsemblBacteria; CAA14671; CAA14671; CAA14671.
DR KEGG; rpr:RP206; -.
DR PATRIC; fig|272947.5.peg.215; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_2_5; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000002480; 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 Reference proteome; Topoisomerase.
FT CHAIN 1..905
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145247"
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; 101081 MW; A715C49A5A2328B6 CRC64;
MIDKYSSNLV PVNIEDEMKV SYLDYAMSVI VSRAIPDVRD GLKPVHRRII YSMYEAGNHA
SKPYRKSARI VGDVMGKYHP HGDSAIYDSL VRMAQDFSLR LPLVDGQGNF GSMDGDAAAA
MRYTESRMAK VAHKLVEDID KGTVSFNINY DGSEEEPSVL PAMFPNLLVN GSGGIAVGMA
TNIPPHNLGE IIDACCLYID NHDIEILDLL EVVKGPDFPT GSMILGISGI RSAYLTGRGS
IIMRGKAEIE NVGNSRQAII ITEIPYMVNK ARLVEKIAEM VKEKRIEGIS DLRDESNKNG
IRIFIELKKD VVAEVVLNQI YACTQLQTNF GVIMLALKDG LPKVMNLKEV IAAFVSFREV
VITNRTIYLL NKARDRAHIL LGLTIAISNI DEIIYIIKAS NDTNLAKQEL MARQWEVLDI
LPLIKLVDDK VILNERGTLS FTEVQAKAIL EMKLQRLTAM EKEKLEQDLK HLATDIAEYL
NILASRTRLL EILKEELIKV KEEFASPRLT SIEFGEFDQD IEDLIQREEM VVTVTLGGYI
KRVPLSSYRS QKRGGKGRSG LSMRDEDITT QVFVGSTHTP MLFFSNIGKV YSLKLYKLPL
SNPQGKGRPM VNILSLQENE HITNIMPLPE NQDEWDHLNI MFATAKGNIR RSDLLDFKKI
QSNGKIAIRL DEDDKLIDVK PCKEDEHILL ATKAGKALRF PVESLRIIKS RISDGVRGMK
LAKEDSVISM TVLKGINSTK EDRDAYLTVP WEKRLEIAKG EEFNLEELGV NLNADSILEM
ANSEEFILTV TENGFGKRSS AYGYRITDRG GSGIINMDIN DKTGLVVGVM PVKMDDELML
ITNSGKLIRC KLESVRITGR NTSGVILFKL DDDEKVVSVS LIAETSESEE ASELAEEGLE
NDVKV
