ID A0A061A854_9MOLU Unreviewed; 867 AA.
AC A0A061A854;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:CDR30080.1};
GN ORFNames=Aocu_00070 {ECO:0000313|EMBL:CDR30080.1};
OS Acholeplasma oculi.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=35623 {ECO:0000313|EMBL:CDR30080.1, ECO:0000313|Proteomes:UP000032434};
RN [1] {ECO:0000313|Proteomes:UP000032434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kube M.;
RL Submitted (MAY-2014) 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; LK028559; CDR30080.1; -; Genomic_DNA.
DR RefSeq; WP_045748689.1; NZ_UFRU01000001.1.
DR AlphaFoldDB; A0A061A854; -.
DR STRING; 35623.Aocu_00070; -.
DR KEGG; aoc:Aocu_00070; -.
DR PATRIC; fig|35623.3.peg.7; -.
DR HOGENOM; CLU_002977_6_1_14; -.
DR InParanoid; A0A061A854; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000032434; 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}; Reference proteome {ECO:0000313|Proteomes:UP000032434};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 15..467
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 529..535
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 867 AA; 97602 MW; 81CAB0B21BCF8475 CRC64;
MSDQKDKLYD KIKEINIASE MKTSFLNYAM SVIVSRALPN AKDGLKPVQR RILYAMHENN
MYANTAHKKS ARIVGDVMGK YHPHGDSSIY DAMVRMAQPF SYRKTLVDGH GNFGSVDGDG
AAAMRYTEAR LSKIAGEMVR DLDKNTVPFV DNYDASEKEP AVLPSRYPNL LVNGSTGIAV
GMATNIPPHN LGEVIDGLFA YIDNPDISVL ELMQYIKGPD FPTGGQILGI NGLRQAYETG
KGIIAVRAKH EFVETKNRTE LIITEIPYMV NKTTLIERIA EVVKNKIIEG ISDLRDESSR
KGMRIVIELK KDVNPMVTLN NLYKHTQLQT SFGINMIALV DGQPKLLSIK DALIHYLAHQ
VDIITRRTEF DLEKAEARMH ILDALVKALS DVDRVIQIIR DAKTPDVARQ GLIDTYAFTD
IQARSILTMQ LQRLTSLEID KIYDETNALK LKISEYKDIL ANEDLKIEII KNELLEIKQK
YDDPRQSEIN LYEDLDIDNE DLIPVEDIVV TVTNNGYIKR MNVDEYKLQN RGGVGMSGVK
LHEDDYVEHI LMTSTHDFHL FFTNKGRVFK LKGYKLPSGS RQSKGVPIVN FLTFQPGEKL
ASFTSIRNFD EENHYLFFVT KNGIVKRTHI SNYQNIRQNG IIALNLKEDD ELLVVKSTDG
NKHILLGASN GKAIHFHEED VREIGRTATG VRGMSLDNND KIVGFAVIDA IEDDILIITE
KGYGKRTSIQ EYRLQNRGGK GVKTLNVTEK NGKLSTLRKV TNDEDLIVVS DKGITIRMPI
NQISQTKRAT QGVRIISLKG DQKVATIAIV PHQEEIKEEI ESAHITQEQM ALNPQKPQVQ
VVELEALASD NETDTDETLE QIKLDLE
//
