ID A0A143XQD0_9FIRM Unreviewed; 829 AA.
AC A0A143XQD0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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_1 {ECO:0000313|EMBL:CVI69109.1};
GN Synonyms=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=NDGK_01431 {ECO:0000313|EMBL:CVI69109.1};
OS Clostridiales bacterium CHKCI001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1780378 {ECO:0000313|EMBL:CVI69109.1, ECO:0000313|Proteomes:UP000198774};
RN [1] {ECO:0000313|EMBL:CVI69109.1, ECO:0000313|Proteomes:UP000198774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHKC1 {ECO:0000313|EMBL:CVI69109.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FCNS01000020; CVI69109.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143XQD0; -.
DR STRING; 1780378.NDGK_01431; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000198774; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000198774};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 12..470
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 442..476
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 531..537
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 829 AA; 92929 MW; EB334A89A6E5771D CRC64;
MDETIFDKVH DVDLKKTMEQ SYIAYAMSVI ASRALPDVRD GLKPVQRRVL YSMIELNNGP
DKPHRKCARI VGDTMGKYHP HGDSSIYGAL VNLAQDWSTR YPLVDGHGNF GSVDGDGAAA
MRYTEARLSK ISMEMLADIN KDTVEFVPNF DETEKEPVVL PSRFPNLLVN GTTGIAVGMA
TNIPPHNLRE TIAAVVKIID NRIQEGRDTA IEEILDIVKG PDFPTGAMVL GRRGIEQAYR
TGKGKIKVRA VTSIEPMANG KHRIVATELP YMVNKARLIE KIAELVKDKR IDGITELRDE
SNREGTRVCI ELRRDVNPNI VLNQLMKHTQ LQDTFGVNML ALVGNQPQIL NLLDMLKYYL
QHQEDVVTRR TRYELNRAQE RAHILEGLLI ALDHIDEVIR IIRGAANVAE AKTKLIQTYG
LSDAQSQAIV DMRLRALTGL ERHKLEAEYE ELMKKIAELK AILSDENRLL AVIKEEITAV
AAKYGDERRT SIGFDEEDFS AEDLIPDENT VIAMTKLGYI KRMSMDNFKA QNRGGRGIKG
MQAIDEDYIE DLLITTTHHY LLFFTNLGRV YRLKTYEIPE AGRTARGTAI VNLIQLQPQE
KVTAIIARRE FNEGEYLFMA TKSGMVKKTD FVEYANIRKV GLAAIHLKEN DELIEVKVTD
NEKDIFLVSK YGQCIRFKET DVRATGRTSM GVIGMNLEDG DEVIGMQLNT QGTDLLFVSE
YGLGKRTSID EFSCQYRGGK GVKCYRINEK SGNIVGVKAV NESQEIMIIT TEGIVIRLKV
SDISLLGRNT SGVKLINIDT ESGVAVASIA KVRESESEVQ EETKELENV
//
