ID D3R2Z9_MAGIU Unreviewed; 867 AA.
AC D3R2Z9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 87.
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:ADC90751.1};
GN OrderedLocusNames=HMPREF0868_1289 {ECO:0000313|EMBL:ADC90751.1};
OS Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS (strain UPII9-5)).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Mageeibacillus.
OX NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC90751.1, ECO:0000313|Proteomes:UP000008234};
RN [1] {ECO:0000313|Proteomes:UP000008234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RT "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL Submitted (DEC-2009) 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; CP001850; ADC90751.1; -; Genomic_DNA.
DR RefSeq; WP_012993063.1; NC_013895.2.
DR AlphaFoldDB; D3R2Z9; -.
DR STRING; 699246.HMPREF0868_1289; -.
DR KEGG; clo:HMPREF0868_1289; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000008234; 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:UP000008234};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 29..488
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 830..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 550..556
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 140
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 867 AA; 97962 MW; 3619283AB42F144D CRC64;
MATTKDNNNS QHNNVDAVFR DNINNIVPVD LEQEMRKSFI DYAMSVISDR ALPDIRDGLK
PVHRRILFSM FSQGFTPDKP YRKCATTVGN VLGHFHPHGD AAVYDSMVRL AQDFSMRHTM
VDGHGNFGSR DGDPPAAYRY TEARLTKIAV EMMRDINKNT VDFKPNFDEQ EMEPIVLPSR
FPNLLVNGST GIAVGMATDI PPHNLGETID AVVMRINNPD CDLEDIMEIL PGPDFPTGGT
ILGLSGIRET YRTGKGRITV RSAASIEDMP NNRHKIVVHD LPYMVNKARL IEKMADLVKE
KRIDGISMIR DESDRNEEIR IVIELKRDAN PQVVLNRLYK MTQLQDNFNA NMLALVPDAQ
GRYEPKVVTL LDCLDHYIAH QKSVVLRRTK FDLDKALARQ HIVQGLLKAI DNIDEVIRII
RSSSNEETAK QALCERFDFS IRQAQHIVDM RLGRLTALER ERLQKELDEL IVKIEYFNRI
INESSLLNQV ICDELTDLKT RYANKRRTVI EPYSLDEFED EELVKEEEVV ITLTHFGYVK
RQPVDTYQQQ HRGGRGISGL QTREDDFVET LVTTSTHDHL LFFTNTGRVF RLKGYQIPEA
GRQAKGQAIV NLLQLVEGEK VRTVITVHEF NREDYLLMAT ARGMIKKTSL YEYANIQKNG
LIAINLRPDD EVIGVKVSRL HEEVILATAG GYSLRFDTND IRNTGRNTFG VSGIKLRHSD
KVIGMAAVDE ERHLLVISKN GYGKRSEFNE YRIQNRGGKG LITYKPTEQT GDLAGIASIN
DEDDIIIIND AGIVIRVATK EIPILSRVTK GVRLMRTAGQ IVDLAVVQHD DEQPNEKPDV
IPDTVDLGLS DGQVAEGTTS VPETDDD
//
