GYRA_BRAHW
ID GYRA_BRAHW Reviewed; 834 AA.
AC C0R046;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BHWA1_01001;
OS Brachyspira hyodysenteriae (strain ATCC 49526 / WA1).
OC Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX NCBI_TaxID=565034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49526 / WA1;
RX PubMed=19262690; DOI=10.1371/journal.pone.0004641;
RA Bellgard M.I., Wanchanthuek P., La T., Ryan K., Moolhuijzen P.,
RA Albertyn Z., Shaban B., Motro Y., Dunn D.S., Schibeci D., Hunter A.,
RA Barrero R., Phillips N.D., Hampson D.J.;
RT "Genome sequence of the pathogenic intestinal spirochete Brachyspira
RT hyodysenteriae reveals adaptations to its lifestyle in the porcine large
RT intestine.";
RL PLoS ONE 4:E4641-E4641(2009).
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; CP001357; ACN83484.1; -; Genomic_DNA.
DR RefSeq; WP_012670533.1; NC_012225.1.
DR AlphaFoldDB; C0R046; -.
DR SMR; C0R046; -.
DR STRING; 565034.BHWA1_01001; -.
DR PRIDE; C0R046; -.
DR EnsemblBacteria; ACN83484; ACN83484; BHWA1_01001.
DR KEGG; bhy:BHWA1_01001; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_12; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000001803; 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..834
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409822"
FT MOTIF 547..553
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 141
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 834 AA; 93275 MW; 3861AF98EF2050EC CRC64;
MAVKKNKEDN SEERQYSTLT KDILKRVDHI SIENELRESY LTYAMSVIVS RALPDVRDGL
KPVHRRILYA MYDANLTHDK PYKKSAATVG EVLARYHPHG DAAVYGTMVR MAQDFSMRYL
LVDGQGNFGS IDDDPPAAMR YTEARMTRFA EEMLNDIEKE TVKFVPNFDD SRTEPSVLPA
TVPQLLVNGS MGIAIGMATN MPPHNLKEVV NAIVYYIDHQ DAEIKDLMRY VQGPDFPTAG
IIYGKEGIKE AYTTGKGRIK LRARLEVEET KRDREAIVVK ELPYGVVKTT LHEKIADLVK
QGKIEGVADI RDESSNRAGI RLIIELKKGV ATQIVLNQLW KHTDLETTFG IINLALVNGE
PKVLNLKELI KYFVDHRVEV ITKRTEYDLN QAKAKAHILE GLLIAQANIE EVIRIIRESE
NTDAARTTLM NRFKLSEKQA QAILDMPLKR LTALEKLKIE QELQQLREFI AYCEDLLAHP
EKILAVIKDE LKKISEKYGD DRRSEIIGKT NDTEIDEEDL IHDEDVAVSI TTQGFIKRVP
ASSYRTQGRG GVGVQGGKSQ GEHYIEHLFV ASTKDYLFIF TDRGKAFWMK VHEIPALSKI
SQGKSIKFIL NLAPEEKITS YFTVSEFDPK QSIIMVTKMG TIKKMELKHL ENAKKRGILA
LTLENNDELV AVSPVQTGDD FIMTTAAGLA LRITEEKIRK MGRAAAGVKG ISLDDDDICV
SGNAIHKGES LIVITENGIG KRLSSKQFNV KGRGGKGQIY IKPDNKTGNV VSVKTVGDKD
EIMVVTTDDM TIKIKADSIP ELGRNAKGVK IVNISDGARV SDLAVVPADN EEKK
