(data stored in SCRATCH3701 zone)

SWISSPROT: 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   11-DEC-2019, entry version 96.
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}.
DR   EMBL; CP000053; AAY61906.1; -; Genomic_DNA.
DR   RefSeq; WP_011271367.1; NC_007109.1.
DR   SMR; Q4UKM1; -.
DR   STRING; 315456.RF_1055; -.
DR   EnsemblBacteria; AAY61906; AAY61906; RF_1055.
DR   KEGG; rfe:RF_1055; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; EIDANKH; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; RFEL315456:G1G4G-1756-MONOMER; -.
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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 1.10.268.10; -; 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; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
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;
DR   PRODOM; Q4UKM1.
DR   SWISS-2DPAGE; Q4UKM1.
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   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
//

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