GenomeNet

Database: UniProt
Entry: A0A1F8ASK7_9BACT
LinkDB: A0A1F8ASK7_9BACT
Original site: A0A1F8ASK7_9BACT 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system