GYRA_MYCGE
ID GYRA_MYCGE Reviewed; 836 AA.
AC P47250; Q49325;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=MG004;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8083173; DOI=10.1128/jb.176.18.5814-5819.1994;
RA Bailey C.C., Bott K.F.;
RT "An unusual gene containing a dnaJ N-terminal box flanks the putative
RT origin of replication of Mycoplasma genitalium.";
RL J. Bacteriol. 176:5814-5819(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77 AND 205-302.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 509-639.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=1945886; DOI=10.1093/nar/19.21.6027;
RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A random sequencing approach for placing markers on the physical map of
RT Mycoplasma genitalium.";
RL Nucleic Acids Res. 19:6027-6031(1991).
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; U09251; AAA57072.1; -; Genomic_DNA.
DR EMBL; L43967; AAC71220.1; -; Genomic_DNA.
DR EMBL; U02211; AAD12504.1; -; Genomic_DNA.
DR EMBL; U01696; AAB01009.1; -; Genomic_DNA.
DR EMBL; X61533; CAA43745.1; -; Genomic_DNA.
DR PIR; D64200; D64200.
DR RefSeq; WP_009885559.1; NZ_AAGX01000001.1.
DR AlphaFoldDB; P47250; -.
DR SMR; P47250; -.
DR STRING; 243273.MG_004; -.
DR PRIDE; P47250; -.
DR EnsemblBacteria; AAC71220; AAC71220; MG_004.
DR KEGG; mge:MG_004; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_14; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR BioCyc; MGEN243273:G1GJ2-4-MON; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
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..836
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145240"
FT MOTIF 537..543
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 134
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT CONFLICT 68..76
FT /note="GMHHDRPFK -> WSCTMIVLL (in Ref. 3; AAD12504)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="R -> L (in Ref. 1; AAA57072)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 93682 MW; 364A78ED5B060BCE CRC64;
MAKQQDQVDK IRENLDNSTV KSISLANELE RSFMEYAMSV IVARALPDAR DGLKPVHRRV
LYGAYIGGMH HDRPFKKSAR IVGDVMSKFH PHGDMAIYDT MSRMAQDFSL RYLLIDGHGN
FGSIDGDRPA AQRYTEARLS KLAAELLKDI DKDTVDFIAN YDGEEKEPTV LPAAFPNLLA
NGSSGIAVGM STSIPSHNLS ELIAGLIMLI DNPQCTFQEL LTVIKGPDFP TGANIIYTKG
IESYFETGKG NVVIRSKVEI EQLQTRSALV VTEIPYMVNK TTLIEKIVEL VKAEEISGIA
DIRDESSREG IRLVIEVKRD TVPEVLLNQL FKSTRLQVRF PVNMLALVKG APVLLNMKQA
LEVYLDHQID VLVRKTKFVL NKQQERYHIL SGLLIAALNI DEVVAIIKKS ANNQEAINTL
NTKFKLDEIQ AKAVLDMRLR SLSVLEVNKL QTEQKELKDS IEFCKKVLAD QKLQLKIIKE
ELQKINDQFG DERRSEILYD ISEEIDDESL IKVENVVITM STNGYLKRIG VDAYNLQHRG
GVGVKGLTTY VDDSISQLLV CSTHSDLLFF TDKGKVYRIR AHQIPYGFRT NKGIPAVNLI
KIEKDERICS LLSVNNYDDG YFFFCTKNGI VKRTSLNEFI NILSNGKRAI SFDDNDTLYS
VIKTHGNDEI FIGSTNGFVV RFHENQLRVL SRTARGVFGI SLNKGEFVNG LSTSSNGSLL
LSVGQNGIGK LTSIDKYRLT KRNAKGVKTL RVTDRTGPVV TTTTVFGNED LLMISSAGKI
VRTSLQELSE QGKNTSGVKL IRLKDNERLE RVTIFKEELE DKEMQLEDVG SKQITQ
