ID A0A3M8H8U9_9BACI Unreviewed; 843 AA.
AC A0A3M8H8U9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 ECO:0000313|EMBL:RNC98857.1};
GN ORFNames=EC501_09435 {ECO:0000313|EMBL:RNC98857.1};
OS Lysinibacillus halotolerans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1368476 {ECO:0000313|EMBL:RNC98857.1, ECO:0000313|Proteomes:UP000279909};
RN [1] {ECO:0000313|EMBL:RNC98857.1, ECO:0000313|Proteomes:UP000279909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A12703 {ECO:0000313|EMBL:RNC98857.1,
RC ECO:0000313|Proteomes:UP000279909};
RX PubMed=24814335; DOI=10.1099/ijs.0.061465-0;
RA Kong D., Wang Y., Zhao B., Li Y., Song J., Zhai Y., Zhang C., Wang H.,
RA Chen X., Zhao B., Ruan Z.;
RT "Lysinibacillus halotolerans sp. nov., isolated from saline-alkaline
RT soil.";
RL Int. J. Syst. Evol. Microbiol. 64:2593-2598(2014).
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:RNC98857.1}.
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DR EMBL; RHLQ01000020; RNC98857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8H8U9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000279909; 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}; Reference proteome {ECO:0000313|Proteomes:UP000279909};
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 REGION 805..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 843 AA; 94597 MW; 16F5A1402B13EDE7 CRC64;
MSENQHEGVK GIKISEEVQT SFLNYAMSVI VSRALPDVRD GLKPVHRRIL YGMHELGNTS
DKPYKKSARI VGDVMGKYHP HGDSSIYDAM VRMAQDFSYR YMLVDGHGNF GSVDGDGAAA
MRYTESRMSK ITMEMLRDIN KDTIDYQANY DGNEKEPIVL PARIPNLLLN GASGIAVGMA
TNIPPHQLGE TIDAVIALSE NPAITTEELM EIIPGPDFPT GGLILGRSGI RRAYETGRGS
ITVRAKAEIE TKSNGKETII VHEIPYQVNK ARLIEKIAEL VRDKKIDGIT NLRDESDRRG
MRIVIEVRKD ANANVILNNL YKQTAMQSNF GVNMLALVNG QPKVLSLKEV LFHYLEHQKV
VITRRTQFEL RKAEDRAHIL EGLRIALDHI DEIISIIRSS RSGDEAKPVL MERFNLTERQ
AQAILDMRLV RLSGLEREKI ENEYQELQVL IAELKAILAD ESKVIDIIRT ELTEIKERYN
DKRRTEITAG GLEMIEDEDL IPREDSVITL THNGYIKRLA SNTYRSQKRG GRGVQGMGTH
EDDFVEHLLF TSTHDTILFF TSKGKVYRAK GYEIPEFGRT AKGLPIVNLL PLEKEEKVTA
MIHVNEFKED AYFIFTTKTG ITKRTQLSQF ANIRTSGLIA IHLHDDDDLI SVRLTDGTKD
VIIGTHDGML IRFKEEEIRS MGRTASGVRG IKLREGDYVV GMEIVEPGQE ILVVTEKGYG
KRTPESEYRL QSRGGVGLKT IQITEKNGPM CAVKTVDGSE DIMLITINGI LIRMDVNDIS
IIGRSTQGVR LIRLSEDELV ATVARVKKDE ETEEDIADED NTTAELNNDS VIDSSETDSE
TEE
//
