ID A0A3Q9HS20_9FIRM Unreviewed; 852 AA.
AC A0A3Q9HS20;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=BBF96_13400 {ECO:0000313|EMBL:AZR74309.1};
OS Anoxybacter fermentans.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR74309.1, ECO:0000313|Proteomes:UP000267250};
RN [1] {ECO:0000313|EMBL:AZR74309.1, ECO:0000313|Proteomes:UP000267250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY22613 {ECO:0000313|EMBL:AZR74309.1,
RC ECO:0000313|Proteomes:UP000267250};
RA Zeng X., Shao Z.;
RT "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT Anoxybacter fermentans.";
RL Submitted (JUL-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; CP016379; AZR74309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3Q9HS20; -.
DR KEGG; aft:BBF96_13400; -.
DR Proteomes; UP000267250; 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}; 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:UP000267250};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 14..467
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 807..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 439..480
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 528..534
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 809..833
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 125
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 852 AA; 96778 MW; CA3CC0973FCD7541 CRC64;
MSMEGIQNDH VKLVGIEDQM KNAYLDYAMS VIVGRALPDV RDGLKPVHRR ILYAMYELGM
YPNKPYKKSA RIVGEVLGKY HPHGDSAVYD TMVRMAQDFS YRYPLIDGHG NFGSIDGDAA
AAMRYTEARM SQITMELLSD IDKNTVDFRP NFDDSLKEPE VLPARLPNLL INGASGIAVG
MATNIPPHNL GEVIDGIIML IDNPEVSIEK LMKVIKGPDF PTGGIIMGRN RIKKAYKTGR
GHLKVRARTN IEEMKNGKHR IVVTEIPYQV NKAKLIEKIA ELVREGKIKG ITDLRDESDR
EGLRIVIELR KDVVPKIVLN QLFKHTRLQV TFGVINLVLV NNEPKVLNLK ELLQEYISHQ
KEVVTRRIKY DLKKAEDKAH ILEGLRIALA DIDRVIQLIR SSKDTAIAKE RLIDTFKMTE
RQAQAILDMR LQRLTGLERE KIEIEYKELL EKIAFYKDVL NDEKKLYGII KEELLELKEK
YADERRTEIV QDYSSLDAED LIPQKDSVIT LTHQGYIKRM PLDLYRSQRR GGRGITGMST
KEEDFVECMI TATTHDYFLF FTNKGLVYRL KGYQIPEASR QSRGTAIVNL LELQPDERVT
AVIPVRNFSE NKYLVTITKN GLIKKTPLVD YESKYTSLIG VTLREGDELI SVRLAEEGQD
IIVGTAHGKA IRFSEREVRS MGRSAQGVKA ITLDPQDYVV GMGVISEGSR ILTVTNKGYG
KLTLESEYRP QTRGGKGLIT IRLTEKNGHL ITLRVVNKEK EIMMISSGGI MIRIPIEEIS
VLGRNTLGVK MMRLDPEDEV VSVALIDPED EKEIEEPEKN DTDIDEIDDL DNDKVDYPDF
IDQEYDEDIG DD
//
