ID A0A1H1Q3W4_9ACTO Unreviewed; 866 AA.
AC A0A1H1Q3W4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=SAMN04489715_1783 {ECO:0000313|EMBL:SDS18115.1};
OS Schaalia meyeri.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=52773 {ECO:0000313|EMBL:SDS18115.1, ECO:0000313|Proteomes:UP000181914};
RN [1] {ECO:0000313|Proteomes:UP000181914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20733 {ECO:0000313|Proteomes:UP000181914};
RA Varghese N.;
RL Submitted (OCT-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; FNLK01000015; SDS18115.1; -; Genomic_DNA.
DR RefSeq; WP_050695498.1; NZ_FNLK01000015.1.
DR AlphaFoldDB; A0A1H1Q3W4; -.
DR STRING; 52773.ADJ76_07675; -.
DR KEGG; amy:ADJ76_07675; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000181914; 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 21..478
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 823..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 539..545
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 842..866
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 866 AA; 96076 MW; 8827A0EF4DBB9D69 CRC64;
MSDEQITDAR HISETERIRQ VDLQKEMQRS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY
AMYDGGYRPT SSFSKSSRVV GEVMGNYHPH GDAAIYDALA RLVQPWSMRY PLVAGQGNFG
TPGNLGPAAP RYTECKMAPL AMEMVRDIDE ECVDFQDNYD GRNKEPTILP ARFPNLLANG
SEGIAVGMAT RIPPHNLREV ARGVEWALAH PEATREELLE ALLTIIPGPD FPTGATILGR
KGIEDAYRTG RGSITQRAVV NVEEIQGRQC LVVTELPYQV NPDNLADKIA QLVRDGQISG
IADIRDETSG RTGQRLVIVL KRDAVAKVVL NNLYKRTPLQ ENFSANMLAL VDGVPRTLSI
DGFIRHWITH QIDVIVRRTR FRLRKALERL HILEGYLKAL DALDDVIALI RRSPTVDEAR
AGLIDLLDVD TVQADAILAL QLRRLAALER QKIMDEHAEL KARVDDLNDI LGTPERQRAI
ISEELTEIVD KFGDERRTRI LPFDGDMSME DLIPEEDVVV TITRDGFAKR TRTDNYRSQK
RGGKGVRGTQ LRGDDVVEHF FVTTTHHWLL FFTNLGRVYR AKAYEIPEGG RDAKGQHVAN
LLAFQPDEHI AQVLAIRTYE DADYLVLATK RGLVKKTPLS LYNSPRSGGI IAINLREDEE
GKSDELVSAQ VVMADEDLIL VSRDGQAVRF TATDDQLRAM GRSTSGVRGM KFRGDDELLS
MEVPHEDTDL LIVTETGYAK RTPVEEYPTK SRGTLGVRVG KLVDERGGLV GALVVRPDED
VMVITESGKL VQVNASDVRP TARNTMGVIF ARPDDGDRII AITRSSDSAG DEDDEDATAE
EAGLADAAKD EAADADGGNA PEESRE
//
