GYRA_MYCGA
ID GYRA_MYCGA Reviewed; 846 AA.
AC P47719;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 130.
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}; OrderedLocusNames=MYCGA7230;
GN ORFNames=MGA_0612;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-384.
RC STRAIN=S6;
RX PubMed=7557470; DOI=10.1016/0378-1119(95)00440-h;
RA Forsyth M.H., Sayed A.S., Geary S.J.;
RT "Sequence and transcriptional analysis of the genes encoding the class-II
RT topoisomerase of Mycoplasma gallisepticum.";
RL Gene 163:161-162(1995).
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; AE015450; AAP57073.1; -; Genomic_DNA.
DR EMBL; U18306; AAA57342.1; -; Genomic_DNA.
DR RefSeq; WP_011113986.1; NC_004829.2.
DR AlphaFoldDB; P47719; -.
DR SMR; P47719; -.
DR PRIDE; P47719; -.
DR KEGG; mga:MGA_0612; -.
DR PATRIC; fig|233150.7.peg.813; -.
DR HOGENOM; CLU_002977_6_1_14; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000001418; 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..846
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145239"
FT REGION 817..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 536..542
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 817..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT CONFLICT 55..57
FT /note="HRR -> TW (in Ref. 2; AAA57342)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="S -> G (in Ref. 2; AAA57342)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> G (in Ref. 2; AAA57342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 94333 MW; A5A16FEAAA5FB683 CRC64;
MNPNDKNNIK ELLNKTVVKE ASITKELETS FMEYAMSVIV SRALPESRDG LKPVHRRVLY
GAYTSGLTHD KPYRKSAQIV GHVMGKYHPH SDSAIYETMV RMAQPFSLRY MLIDGHGNFG
SIDGDSAAAM RYTEARLSKI SAEMLRNIDK DTVDFVDNYD ASEQEPIVLP SLFPNLLANG
SSGIAVGMAT NIPPHNLSEL IGGIKHLLVN ENATIEELKE FIKGPDFPTA AEILGETGIN
EYFNTGRGSV SVRAKSEIEE LANNKSNIVI TQIPYMVNKA NLINKIAELV KTEQIQGIAD
LRDESNREGI RIVIETKRDV IPEVLLNQLY KSTQLQTNFS VAMLALVNNQ PKVLNLKEAL
QIYIDHQFDI LLRKTNFELK KAKASAHIVE GLVIATNNID DVIETIKNAK DNEDAKNTLM
TKYELSDLQA KAILDMRLRS LSGLERENLQ KELAKLKELI KDLEEILQNK ERRIKIISDQ
LDEIDHKFGD ERRTKICYGL NSTIDNEQLI PVETVVITRS SKGYLKRIPI SAYKVQHRGG
VGVKGMNTYE DDDVESLIVC STHSDLLFFT NYGKVYRIRA HQVPLGSRIS KGIPAINLIS
IEKDEKLMSL LSINDYDSGY FFFSTKKGLV KRVKASEFSR IQNNGKIAIK LTENDSLFKV
IKTAGDEEIY IGVSSGLLVR FKEDVVRSMG RTAQGVIGVK FKNPNDEVIG LSSSHEGSLL
LAVCEKGVGK MTDREEYRMT NRGSKGVITI KVTPKTGNII NTQLVNGNEE LLMISSTGKI
VRVPLAEVSE QGRNTSGVKL ISLNEKETLQ SVAIFDVEQD DSQQVGSDNP DTELSSDDSN
QDQDKE
