ID A0A022KW07_9MICO Unreviewed; 962 AA.
AC A0A022KW07;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=D641_0109920 {ECO:0000313|EMBL:EYT48947.1};
OS Brachybacterium muris UCD-AY4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT48947.1, ECO:0000313|Proteomes:UP000019754};
RN [1] {ECO:0000313|EMBL:EYT48947.1, ECO:0000313|Proteomes:UP000019754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT48947.1,
RC ECO:0000313|Proteomes:UP000019754};
RX PubMed=23516213;
RA Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT UCD-AY4.";
RL Genome Announc. 1:E0008613-E0008613(2013).
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:EYT48947.1}.
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DR EMBL; AORC01000011; EYT48947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022KW07; -.
DR STRING; 1249481.D641_0109920; -.
DR HOGENOM; CLU_002977_6_1_11; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000019754; 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:UP000019754};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 82..539
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 907..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 600..606
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 909..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 962 AA; 105436 MW; D54162AF1F9FE258 CRC64;
MSDTPNDPTT PGENVGDDTP VEPGADATTP EASSEDTRLD GAPATGIGPA GTTEISASEA
TDRTVTLVDP LDENEVDKIS QVDLNQEMQR SYLDYAMSVI VGRALPDVRD GLKPVHRRII
YAMFDGGYRP DRSFSKCAKV VGEVMGNYHP HGDSAIYDAM VRLVQPWSMR YPLILGQGNF
GSAGDDGAAA PRYTECKMAP LALELVRDID QDTVDVQDNY DGTISEPVVL PARFPNLLVN
GSSGIAVGMA TNIPPHNLRE VAEAVQWLLQ NHEATKPELL DACLRFIKGP DFPTGATIVG
TKGIEEAYRT GRGSITQRAV VSTEEINGRM SLVVTELPYQ VNPDTLARKI AELVKLGKMQ
GIADITDETS GRTGQRLVIT LKRDAVAKVV LNNLYKHTQL QENFSANMLA LAGGVPRTLS
IDSFVREWTR HQIDVIVRRT QYRLRKAQEQ IHIYRGYLKA LDALDEVIAL IRRSPDADQA
RTGLMEMLEI DEVQANAILA MQLRRLAALE RQKIIDEHDR LQAMIEEYEG ILADPAWQRR
IVSEELAEIV EKYGDDRRTQ ILPFDSDMSM EDLIPEEDVV VTITKGGYVK RTRTDQYRAQ
KRGGKGVRGA SLRADDVVEH FFTTTTHRWL LFFTNQGRVY RSKGYEIPEA PRDAKGQHVA
NLMAFQPDER IASVLSLDTY EDAEFLVLAT RSGLVKKTPL SAFDSNRTGG IIAINLREVD
GPDGPRPDRV IAARAVNSDD HLLMVSRNGQ SVRFPAADDV LRPMGRATSG VTGMKFRHDD
ELLAMDVVRP GTFVVTVTDG GFAKRTSIDE YRLQGRGGLG IRVAKLPDDR GHLVGAAVVQ
ETDELLVVME RGKVVRSRVD GVPPKGRTTM GVVFAKPDKG DHIILVTTTA EAEVDDDLEA
DEVAEAVEGT QNATENATES ATGEDPMEES ADAASLEPSP EGDALGSDAS EPSSDDDTLN
EE
//
