ID A0A0M2GQT4_9ACTN Unreviewed; 864 AA.
AC A0A0M2GQT4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=UK15_07570 {ECO:0000313|EMBL:KJK40207.1};
OS Streptomyces variegatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=284040 {ECO:0000313|EMBL:KJK40207.1, ECO:0000313|Proteomes:UP000034786};
RN [1] {ECO:0000313|Proteomes:UP000034786}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16380 {ECO:0000313|Proteomes:UP000034786};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJK40207.1}.
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DR EMBL; JYJH01000004; KJK40207.1; -; Genomic_DNA.
DR RefSeq; WP_031137657.1; NZ_JYJH01000004.1.
DR AlphaFoldDB; A0A0M2GQT4; -.
DR STRING; 284040.UK15_07570; -.
DR PATRIC; fig|284040.3.peg.4802; -.
DR Proteomes; UP000034786; 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 23..480
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 832..864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 541..547
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 134
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 864 AA; 95177 MW; A44D2E9A4519FEE7 CRC64;
MTDENTPVTT PEGDALAMRV EPVGLETEMQ RSYLDYAMSV IVSRALPDVR DGLKPVHRRV
LYAMYDGGYR PERGFYKCAR VVGDVMGNYH PHGDSSIYDA LVRLAQSWSM RMPLVDSNGN
FGSPGNDPAA AMRYTECKMA PLSMEMVRDI DEETVDFTDN YDGRSQEPTV LPARFPNLLI
NGSAGIAVGM ATNIPPHNLR EVASGAQWYL ENPEASHEEL LDALIERIKG PDFPTGALVV
GRRGIEEAYR TGRGSITMRA VVEVEEIQNR QCLVVTELPY QVNPDNLAQK IADLVKDGKI
GGIADVRDET SSRTGQRLVI VLKRDAVAKV VLNNLYKHTD LQTNFGANML ALVDGVPRTL
SLDAFIRHWV THQIEVIVRR TRFRLRKAEE RAHILRGLLK ALDAIDEVIA LIRRSDTVDI
ARGGLMSLLE IDEIQANAIL EMQLRRLAAL ERQKIVQEHD ELQAKINEYN EILASPVRQR
GIVSAELAAI VEKFGDDRKT TLIPYEGDMS IEDLIAEEDI VVTVTRGGYI KRTKTDDYRA
QKRGGKGVRG TKLKEDDIVD HFFVSTTHHW LLFFTNKGRV YRVKGYELPD AGRDARGQHV
ANLLAFQPDE AIAEILAIRD YEAVPYLVLA TKAGLVKKTP LKDYDSPRSG GVIAINLREG
QDGSDDELIG AELVSADDDL LLISKKAQSI RFTASDDTLR PMGRATSGVK GMSFREGDEL
LSMNVVRPGT FVFTATDGGY AKRTNVDEYR VQGRGGLGIK AAKIVEDRGS LVGALVVEET
DEILAITLSG GVIRTRVNEI RETGRDTMGV QLINLGKRDA VVGVARNAEA GREAEEVDGD
VVVDDTAEGA VVTGTDEGEA PSAE
//
