ID Q4A580_MYCS5 Unreviewed; 650 AA.
AC Q4A580;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN Name=gyrB {ECO:0000313|EMBL:AAZ44091.1};
GN OrderedLocusNames=MS53_0684 {ECO:0000313|EMBL:AAZ44091.1};
OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=262723 {ECO:0000313|EMBL:AAZ44091.1, ECO:0000313|Proteomes:UP000000549};
RN [1] {ECO:0000313|EMBL:AAZ44091.1, ECO:0000313|Proteomes:UP000000549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53 {ECO:0000313|EMBL:AAZ44091.1,
RC ECO:0000313|Proteomes:UP000000549};
RX PubMed=16077101; DOI=10.1128/JB.187.16.5568-5577.2005;
RA Vasconcelos A.T., Ferreira H.B., Bizarro C.V., Bonatto S.L., Carvalho M.O.,
RA Pinto P.M., Almeida D.F., Almeida L.G., Almeida R., Alves-Filho L.,
RA Assuncao E.N., Azevedo V.A., Bogo M.R., Brigido M.M., Brocchi M.,
RA Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S., Carraro D.M.,
RA de Mattos Cascardo J.C., Castro L.A., Cavalcanti G., Chemale G.,
RA Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.,
RA Fiorentin L., Franco G.R., Freitas N.S., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F., Lopes M.I., Loreto E.L., Madeira H.M.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R., Moreira M.A.,
RA Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C., Paixao R.F.,
RA Pedrosa F.O., Pena S.D., Pereira M., Pereira-Ferrari L., Piffer I.,
RA Pinto L.S., Potrich D.P., Salim A.C., Santos F.R., Schmitt R.,
RA Schneider M.P., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M., Souza K.R., Souza R.C.,
RA Staats C.C., Steffens M.B., Teixeira S.M., Urmenyi T.P., Vainstein M.H.,
RA Zuccherato L.W., Simpson A.J., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; AE017245; AAZ44091.1; -; Genomic_DNA.
DR RefSeq; WP_011283820.1; NC_007294.1.
DR AlphaFoldDB; Q4A580; -.
DR STRING; 262723.MS53_0684; -.
DR KEGG; msy:MS53_0684; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_4_1_14; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000000549; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAZ44091.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000000549};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 433..547
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 405..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73532 MW; F19B8641558151A3 CRC64;
MEDKNKVQNN AEYNADSIEV LEGLEAVRMR PGMYIGSKDK TGLHHLIWEI VDNSVDEVLA
GYADNIKITI TKDGGVSVED NGRGIPVDMH SKGKSALEIV FTGLHAGGKF KSDAYKVSGG
LHGVGASVVN GLSSYLGVWV KRNGNVYFAE FKDGGKLEAP IKVIETTGDN KTGTKVLFYP
DFTIMDKNEF DKNLIVDRIR QTAYLNKNLR ISLSDERDNS FVEFCYPNGI LDFLTVITKS
KNTLQNDELI YTEGIYQDKT GDVKVEIAMR YMASAAKSNA VAYAYTNNIY NKEGGTHLNG
FFNGLTRIWN NYAQDKKFFK TQGEKFSRED LENNLFLIIS IKHNNPEFEG QTKHKLNSRN
ASPAVNKVFS EVFEKTLDQN PKFAEEVIKY LLDFKARRLK DEKEKELQKK KGLGNSSLPG
KLSDCSSKNA EESELYIVEG NSAGGSAKMG RDRHFQAILP LKGKILNVEK KDIEKILKND
EILSLIAALG AGVGQDFNVN KVRYQKVIIM TDADSDGSHI RVLLITFFFK LFRQLIEYGM
LYIAQPPLYK IESNKKVYYA YNEAQKEEIL DSLDKSKKIM IQRYKGLGEM NADQLWETTM
DPKTRKMLQV QVSDAEKAME VLNILMGEET EPRKEFIFEN AKKVRDIDWI
//
