GYRA_GRABC
ID GYRA_GRABC Reviewed; 940 AA.
AC Q0BST5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, 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};
GN OrderedLocusNames=GbCGDNIH1_1219;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI62117.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BST5; -.
DR SMR; Q0BST5; -.
DR STRING; 391165.GbCGDNIH1_1219; -.
DR PRIDE; Q0BST5; -.
DR EnsemblBacteria; ABI62117; ABI62117; GbCGDNIH1_1219.
DR KEGG; gbe:GbCGDNIH1_1219; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_5; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000001963; 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..940
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409825"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 565..571
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 136
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 940 AA; 103175 MW; D0E0C4983DD1ABD5 CRC64;
MSDHTNPPSA PPDDDPNGGS LLMPVTLEEE MSRSYLDYAM SVIVSRALPD ARDGLKPVHR
RILYGMQESG YTADKPYRKS ARINGDVMGK YHPHGDAAIY DALVRLAQPF SLRVPLIDGQ
GNFGSMDGDP AAAPRYTEAR LARSASFLLN DIDRDTVDFQ PNYDDSEMEP RVLPASYPNL
LVNGADGIAV GMATKIPTHN PTEVIDATLA MIDNPDITLD ELMTVIPGPD FPTGGLILGR
SGIRSAFETG KGSITVRART DFEEVRGGRQ AIVISEIPYQ VNKATLQERM AELVRAKQIE
GISDIRDESD RSGVRVVIEL KRDATPDVVL NHLFRFTQLQ ISYGINMLAL DGGQPRLMGL
RDVLSTFIRF REDVILRRAR FELNKARDRA HLLVGLAIAV ANIDEVIRLI RQSPDSTSAR
IALMERDWPA ADVAPLLTLI DDGGNVLTEA QTVRLTEVQA RGILELRLQR LTGLERDKIH
NEMQEVAARI GELLEIIGSH IRRMEVMREE LAVIRAELNS PRRSEINDSL ADQDDESLIE
PGQMVVTITR DGFIKRTPLD VFRQQHRGGR GRAAASMRGD DIVTRSFNAH THQWVLFFSS
GGKAYRQKVW RLPEAGPTAK GRALVNLLPE LGSDGITAVL PLPQDESLWE GLHLVFATAS
GGIRRNRLSD FKNVRASGLI AMKLDEGDRL IGVATCREGD DIMLASRLGR CIRFQANEDT
LRVFAGRESS GVRGMKLAQG DEVISLSVLR HVEATPEERA AYLRYASARR RSAAGEEDQI
DAEVMEADDS EVTVDDTALS PERIAGLEEA EEFLLTVTIA GFGKRSSAYD YRVSGRGGQG
IANINLAPRN GRAVAATFPV RPGDDVMLVT DAGRLIRVPA DQVRITGRST MGVTLFRVDK
DEVVTSVFPV LETESVDDNG DDADSVAPAA PDGQVTDSDD
