ID A0A1P8UBY2_9MICO Unreviewed; 863 AA.
AC A0A1P8UBY2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=BOH66_16490 {ECO:0000313|EMBL:APZ35648.1};
OS Microbacterium aurum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=36805 {ECO:0000313|EMBL:APZ35648.1, ECO:0000313|Proteomes:UP000187185};
RN [1] {ECO:0000313|EMBL:APZ35648.1, ECO:0000313|Proteomes:UP000187185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 15219 {ECO:0000313|EMBL:APZ35648.1,
RC ECO:0000313|Proteomes:UP000187185};
RA Jung Y., Shin J.-H., Lee Y.-J., Yi H., Bahn Y.-S., Kim J.F., Lee D.-W.;
RT "Complete genome sequence of Microbacterium aurum KACC 15219.";
RL Submitted (DEC-2016) 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}.
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DR EMBL; CP018762; APZ35648.1; -; Genomic_DNA.
DR RefSeq; WP_076692005.1; NZ_JAFBCQ010000001.1.
DR AlphaFoldDB; A0A1P8UBY2; -.
DR STRING; 36805.BOH66_16490; -.
DR KEGG; maur:BOH66_16490; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000187185; 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; 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:UP000187185};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 21..478
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 827..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 540..546
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 827..841
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 863 AA; 95373 MW; 6977803A92C8E9B8 CRC64;
MTDDVRPDPN AGHNHGNIDQ VDLQVEMQRS YLDYAMSVIV GRALPDVRDG LKPVHRRVIY
GMYDGGYRPD KSFNKCARIV GEVMGQYHPH GDSAIYDALV RLVQPWSLRY PLAEGQGNFG
SPGNQGAAAP RYTETKMSQL AMEMVRDIDE ETVDFEANYD GKTQEPTVLP SRFPNLLVNG
SVGIAVGMAT NIPPHNLREV AEAALWALEN PDAPREELLE ALMSRVHGPD FPTGAQILGT
KGIRDAQRTG RGSITMRAVV NVEEIQGRTC LVITELPYQV NPDNVALKIR DLARDGRITG
IADIRDETSD RTGQRLVIVL KRDAVAKVVL NNLYKHTQLQ ENFGANMLAI VDGVPRTLAL
DGFITYWIDH QIEVIVRRTQ YRLNEAEKRM HILRGYLKAL DALDEVIALI RRSPTADDAR
EGLKTLLEID DDQANAILSM QLRRLAALER QKIIDEATEL ELKIADLTDI LASPVRQRTI
ISEELTGIVE RFGDDRRTHI LHGFDGDMSM EDLIPEEEMV ITVTRDGYIK RTRSDNYRSQ
HRGGKGVKGA QLRADDVVEH FFVTTTHHWL LFFTTKGRVY RCKAYEVPEA GRDAKGQHVA
NLLALQPGEE IAQILDIRDY KVAQYLVLAT RDGKIKKTAL SEYDTNRQGG IIAIRLRGQE
DAEGGDELVS ALLVDDTDDI LLISRQGMSL RFTATDDSLR PMGRSTEGVK GMSFREGDTL
LSASVAKDEG YVFVVTEGGY AKRTAVDQYR LQGRGGLGIK VAKLNDDRGS LAGGLIAAED
DEVLVVLASG KVVRSAVAEV PAKGRDTMGV VFARPDDDDR ILAIARNGER ALRHEQEPAE
NADAADAADD PSTASPEGSD TDA
//
