ID A0A1F8ASK7_9BACT Unreviewed; 882 AA.
AC A0A1F8ASK7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 24.
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=A3E44_00635 {ECO:0000313|EMBL:OGM54175.1};
OS Candidatus Woesebacteria bacterium RIFCSPHIGHO2_12_FULL_41_24.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802510 {ECO:0000313|EMBL:OGM54175.1, ECO:0000313|Proteomes:UP000178603};
RN [1] {ECO:0000313|EMBL:OGM54175.1, ECO:0000313|Proteomes:UP000178603}
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 topoisomerase GyrA/ParC subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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:OGM54175.1}.
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DR EMBL; MGGW01000017; OGM54175.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8ASK7; -.
DR Proteomes; UP000178603; 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; 2.
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 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; 2.
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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 7..518
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 580..586
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 118
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 882 AA; 97690 MW; 02CDE4EF4ADA63CC CRC64;
MAKVLPTEIT KEVQKSYLDY AMSVIVARAL PDIRDGLKPV HRRILYAMHS MGLSHGSNFS
KTAKVVGEVL GKYHPHGDMA IYDALVRMAQ DFTLRYPLVQ GQGNFGSVDG DPPAAMRYTE
ARLAAIAETI LRDIEHDTVD FGDNFDATLK EPIYLPALLP NLLLMGSEGI AVGMATKIPT
HNLSEVVDAV ITTVKKGKIV SEEVKTKAKA DFFIKKINLI ASGEEKKIEE KDLSNTEVGF
ESEVTIDELT DILPGPDFPT GGAIYDALAL KEVYASGRGK IVVRGIAEIK DLSSQAGGKE
SLPTGRQGKT QIIISEIPYQ VNKAELVAKI AELVKDKKLV GIAGLRDESD KDGMRVAIDL
KRDARAKSVL NNIYKHTKLQ TTFPANFVAL VDGTPHTVNL KQILVEYIRH RQRVVTRRTI
FELTAAKKRA HILEGLKIAL DNLDAVIKTI RESKTQEDAK NALIKRFGLT EIQSNAILDM
QLRRLAALER QKIEDEYEGI KKLIDELSFI LQNPKEVLNI IVKEIQELKA KYGDPRKTKI
YKQKLGEFSE EDLVAKEDVL ITITKTGYIK RVPRGTYKAQ RRGGKGVVGM TTKEEDEIEL
FASASTHDTL LFFTDKGRVF GNKVWEIPES SRQSKGQALV NFINLESGEQ IRSILPMTGG
QYLIMATSRG VVKKTAVKEY QNLRTNGLIA IKLSSDDKLI SVRATNGDDH VLLITKRGKS
IKFPEKNVRG MGRATTGVRG IRLNTEDEVI AMEVFPEKLI IPPDKRKKVY RDILTISVNG
LGKRTKVELF PVQKRGGKGV KAAVANDKTG NLVSADLIDQ NVEQMVITSK HGQVIKLPAK
NIPQLGRATQ GVILMRFAKK DDSVAAVTTL TKTNEDEEPS PY
//