ID A0A1G2RLE6_9BACT Unreviewed; 835 AA.
AC A0A1G2RLE6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=A3B24_00925 {ECO:0000313|EMBL:OHA73189.1};
OS Candidatus Wildermuthbacteria bacterium RIFCSPLOWO2_01_FULL_48_16.
OC Bacteria; Candidatus Wildermuthbacteria.
OX NCBI_TaxID=1802461 {ECO:0000313|EMBL:OHA73189.1, ECO:0000313|Proteomes:UP000176917};
RN [1] {ECO:0000313|EMBL:OHA73189.1, ECO:0000313|Proteomes:UP000176917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OHA73189.1}.
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DR EMBL; MHUG01000015; OHA73189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2RLE6; -.
DR STRING; 1802461.A3B24_00925; -.
DR Proteomes; UP000176917; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 22..483
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 448..475
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 545..551
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 133
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 835 AA; 93376 MW; B910202AD5384F29 CRC64;
MAKEEKENPP AGGTAIGAVK DREIVEEMRS SYLDYAMSVI VARALPDVRD GLKPVHRRIL
FAMQEEGLTH AAKFRKSATV VGAVLGRYHP HGDVAVYDSM VRMAQDFSMR YPLVEGQGNF
GSIDGDPPAA MRYSEARMAR LGELTLQDIE KDTVDFVDNY DGTRREPTVL PSPLPQLLLN
GTLGIAVGMA TNIPPHNLTE VVDALLYLIE HPKADTEDLF QFVKGPDFPT GGTIFNKQEI
IQAYSQGKGP IVVRGKIDVV EEDPSKRSGQ ARTPQIIITE IPYQVVKSSL LEQFAKLVQE
KKVEGIKDIR DESDKDGMRV VFDLQRDAYP QKIINRLYKF SDLQKTFHLN LLALVDGIQP
KVLSLADMLS FFIEHRRVVV TRRTKWELTK AKEREHILEG LWKALSNIDK VIALIRKAED
REDAKVKLMK AFKLTEIQAN AILDMRLSQL ARLERNKIED ELKAIRARIK ELMTILASPK
KIDEVVVKEF KELKETYKDE RRTKVVASAV GEIAEVDLIP QEDTIVTLTQ GGYIKRINPA
TYKIQKRGGK GIVGMKTMGE DIVEHFLYGQ THDHMMVFTD SGKLFQTPVY EIPEGTRVSK
GRGLLNFVDI TSEDRVLTLF AIGKDDIQAG IKNLVFVTKD GVIKKSELDD FKNVRRSGLI
AITLKKGDLL RGVQKTTGED ELIIVTKLGQ SIRFKEKDVR VMGRTAAGIR AIRLKKGDEV
VGMNVIPSLD SKEQKVDYLF ILSENGYGKK TDVKEYRLQT RGGSGIKTAN VTPKTGNLVF
ANILNGQEED LIVISRKGQV IRTAVTSIPK ISRSTQGVRI MRLDPGDKVA SAACL
//
