GYRA_META1
ID GYRA_META1 Reviewed; 898 AA.
AC B3PN30;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
GN OrderedLocusNames=MARTH_orf662;
OS Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=243272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=158L3-1;
RX PubMed=18573899; DOI=10.1128/iai.00516-08;
RA Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA Loraine A.E.;
RT "Genome of Mycoplasma arthritidis.";
RL Infect. Immun. 76:4000-4008(2008).
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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; CP001047; ACF07432.1; -; Genomic_DNA.
DR RefSeq; WP_012498389.1; NC_011025.1.
DR AlphaFoldDB; B3PN30; -.
DR SMR; B3PN30; -.
DR STRING; 243272.MARTH_orf662; -.
DR EnsemblBacteria; ACF07432; ACF07432; MARTH_orf662.
DR KEGG; mat:MARTH_orf662; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_14; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000008812; 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; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 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 Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..898
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409829"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 589..595
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 185
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 898 AA; 100871 MW; 2551E9687F2C54D3 CRC64;
MSDDKKDEEK LKKSDENFDD DSKYYEFDDT IKKVFEEEKA KEEDEDEEEI PQEKEGYQVK
SQLLETEQNG LQPADLAKVM KSSFIEYAMS VIVSRALPDA RDGLKPVHRR ILYGMSELGM
FHTAPHKKSA RIVGDVLGKY HPHGDSSVYE AMVRMAQDFS LRYPLIDGHG NFGSIDGDEA
AAMRYTEARM SKIAGVMVDG IKKNTVDFID NYDGTEKEPT VLPSRFPNLL VSGTSGIAVG
MATNIPPHNL GEIIDAVCAL AKNPEITIDG LMEFVLAPDF PTGATIFNKA GLIEAYKTGR
GSITMRAKAN IQELANGKSK IIITEIPYEV KKTEIMEKIA DHLKNKRIEG ISDFRDESNR
DGIRVVIDVK KNAVPEVILN TLYKLTRLQT NFSFNMIALV NGEPKLLNLK ECLQVYLDHQ
IDVTRRRLQF DLEKDLARAH ILEGLKICVE NIDRVIEIIK KSKTDVDAQA KLCQTFSLSE
IQAKAIVDMR LGRLTGLAIE KMNDELDQVN ARIAEYRAIL SSHEKLIELI IKELQEVKEA
YGDKRRSEIR WDVMSSINNE DLIPQKEIVI TLSSNNYIKR IDLEEYREQR RGGVGVSTVK
TYQDDDIQDV VVANTHADLL IFTDEAKIYR VRGHEIPSGT KQSKGTPIVN IVPTIQKNEK
VVKIICVTDY EESQSLITVT ERGVIKKTNL KEYELIRKNG KYALSLLEDD HLIDVRVVDQ
DEEIFIAASN SRINRFNVAD VREMGRVARG VGGIRLSDDD KVVSVSSSKD GAYIFSLGAK
GYGKLSLVES YRKTKRNAKG VITLNEDKAG KLVYAAAVHG VEDLIIMTQS GIAIRISLRD
INVIGRNAKG VKIINLKGRS DQIVGVAKIY DEDATDRELT KEEYIEVTKE IDIDLANE
