ID R7Z9T7_LYSSH Unreviewed; 823 AA.
AC R7Z9T7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=H131_19197 {ECO:0000313|EMBL:EON70925.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON70925.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON70925.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON70925.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EON70925.1}.
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DR EMBL; AQPX01000026; EON70925.1; -; Genomic_DNA.
DR RefSeq; WP_010860744.1; NZ_KB933398.1.
DR AlphaFoldDB; R7Z9T7; -.
DR PATRIC; fig|1285586.5.peg.4001; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000013911; Unassembled WGS sequence.
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; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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 NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 12..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 527..533
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 823 AA; 91909 MW; 512B78D833E45E00 CRC64;
MSEQERSGVK GINITEEIET SFLDYAMSVI VSRALPDVRD GLKPVHRRIL YGMQELGNTA
DKAYKKSARI VGDVMGKFHP HGDSSIYDAM VRMAQDFSYR YMLVDGHGNF GSVDGDGAAA
MRYTESRMSR IAMEMLRDIN KNTIDYTDNY DGSEKEPVVL PSRYPNLLVN GAAGIAVGMA
TNIPPHQLGE TIDAVLALSE NPAITTEELM EIIPGPDFPT GGLILGRSGI RRAYETGRGS
IIIRAKVEIE QKANGKETIL IHELPYQVNK AKLIEKIAEL VRDKKIDGIT NLRDESDRRG
MRVVIEVRKD ANANVVLNNL YKQTAMQSSF GINMLSLVSG QPKVMGLKEM LYHYLEHQKV
IIRRRTEFDL KKAEDRAHIL EGLRIALDHI DEIIAIIRGS RSGDEAKPQL MERFNLSERQ
AQAILDMRLV RLSGLEREKI EAEYQELQVL IAELKAILAD EAKIVEIIRT EIIEVKERFN
DTRRTEITSG GMEMIEDEDL IPVENSVVTL THNGYIKRLA ANTYRSQKRG GRGVQGMGTN
EDDFVEHLMN TSTHDTILFF TSKGKVFRAK GYEIPEYGRT AKGLPIVNLL NIEKDEKVTA
MIRVASFEDD AYFIFTTKTG ITKRTPVSQF ANIRTNGLIA ISLREDDDLI AVRLTDGSKQ
VIIGTRDGML VRFQEDDIRS MGRTAGGVRG IKLRDGDEVV GMEIVESGEE ILVVTAKGYG
KRTSEEEYRL QSRGGVGLKT IQITDKNGPM VAVKTVDGSE DLMLITINGM LIRMDVNDIS
LIGRSTQGVR LIRLGDDELV ATVAKVEKEE DDDSSEDDEQ VVE
//
