ID A0A060Q0F8_9RICK Unreviewed; 903 AA.
AC A0A060Q0F8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 ECO:0000313|EMBL:BAP00057.1};
GN ORFNames=WCLE_007610 {ECO:0000313|EMBL:BAP00057.1};
OS Wolbachia endosymbiont of Cimex lectularius.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=246273 {ECO:0000313|EMBL:BAP00057.1, ECO:0000313|Proteomes:UP000031663};
RN [1] {ECO:0000313|EMBL:BAP00057.1, ECO:0000313|Proteomes:UP000031663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=wCle {ECO:0000313|Proteomes:UP000031663};
RX PubMed=24982177; DOI=10.1073/pnas.1409284111;
RA Nikoh N., Hosokawa T., Moriyama M., Oshima K., Hattori M., Fukatsu T.;
RT "Evolutionary origin of insect-Wolbachia nutritional mutualism.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:10257-10262(2014).
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; AP013028; BAP00057.1; -; Genomic_DNA.
DR RefSeq; WP_041045912.1; NZ_AP013028.1.
DR AlphaFoldDB; A0A060Q0F8; -.
DR STRING; 246273.WCLE_007610; -.
DR KEGG; wcl:WCLE_007610; -.
DR HOGENOM; CLU_002977_6_2_5; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000031663; 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}; 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 8..487
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 876..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 548..554
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 903 AA; 99983 MW; 1DD08D06E6574110 CRC64;
MQDNIVPVSI VKELEDSYLS YAMSVIISRA IPDVRDGFKP VHRRILYAMS RAGYDAGKPY
KKAARIVGDV MGKYHPHGDM AIYDSLVRMA QNFSLLLPLI DGQGNFGSID GDPPASMRYT
EARLHKVSHF LLNDIDEDTV DFRPNYDGNE TEPVVLPAEF PNLLVNGASG VAVGMATNIP
SHNLGEIIDA CMLYIDNPEV TLDELLEVVP GPDFPTGGTI LGRSGIRSAF ATGRGSIVVQ
GKTHIEDLPQ DRQAIVIDEI PYQVNKVKLI EKIGELVKEK KIDGITEIRD ESDKSGIRVV
IDLRKNTAAD FILNQILGLT PLRSSFSVNT LVLSNNRPAL MSLKGIIAAF VDFRKEVLIR
RTEFRLRKTR EKAHIYIGLY IAVLSIDEVI KIIRGAKDPE EASKELLNKE WKTSAEINTI
ISLISDSESF LKDGVYRLTE LQTKAILDMK LQRLTGLEKV KLEAELNSMI NLIKEYIAFL
GSEEGLMKEI KNNLQEIKNR FAVPRKTSIE ESDVDIEAED LIPQEDMVVT VTMNGYIKRV
KLSHYRTQRR GGKGKLGQGL KEEDVTTKLF VGNTHTSLLF FSNIGRVYRL KVYKLPLAEP
TARGRALVNV FPLTEGETIT NIMPLPSEND ENQNIVFATA HGNIRRNSLA DFHYIPSNGK
IAIKLDGGDK LVSVKVCNEI DHVLLSTTLG KSIRFVVSDV RQFKSRNSDG VRGIKLVKSD
SVISMTILNG IGVTTETKEL YLKVPLAKRL EAATNNAIDS KLEKTLNDLG IDSELFLKLA
VNEEFILTIT ENGFGKRTSA YEYRVTNRGG VGITNILTTS RNGSVVASFP VEQGDNIMLI
TDKGKLIRIS VDDIRIAGRS TQGVTLFKTE SKEKVVSAAK IEDPGSTEDS TSEEVGNSVS
SEL
//
