ID   Q8DQB5_STRR6            Unreviewed;       647 AA.
AC   Q8DQB5;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 150.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00939};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
GN   Name=parE {ECO:0000256|HAMAP-Rule:MF_00939,
GN   ECO:0000313|EMBL:AAK99560.1};
GN   OrderedLocusNames=spr0756 {ECO:0000313|EMBL:AAK99560.1};
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101 {ECO:0000313|EMBL:AAK99560.1, ECO:0000313|Proteomes:UP000000586};
RN   [1] {ECO:0000313|EMBL:AAK99560.1, ECO:0000313|Proteomes:UP000000586}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6 {ECO:0000313|Proteomes:UP000000586};
RX   PubMed=11544234; DOI=10.1128/JB.183.19.5709-5717.2001;
RA   Hoskins J.A., Alborn W.Jr., Arnold J., Blaszczak L., Burgett S.,
RA   DeHoff B.S., Estrem S., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A., LaGace R., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S., McHenney M.,
RA   McLeaster K., Mundy C., Nicas T.I., Norris F.H., O'Gara M., Peery R.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C., Baltz R.H., Jaskunas S.Richard.,
RA   Rosteck P.R.Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2] {ECO:0007829|PDB:4LP0, ECO:0007829|PDB:4LPB}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.
RX   PubMed=24098982; DOI=10.1021/jm401208b;
RA   Basarab G.S., Manchester J.I., Bist S., Boriack-Sjodin P.A., Dangel B.,
RA   Illingworth R., Sherer B.A., Sriram S., Uria-Nickelsen M., Eakin A.E.;
RT   "Fragment-to-hit-to-lead discovery of a novel pyridylurea scaffold of ATP
RT   competitive dual targeting type II topoisomerase inhibiting antibacterial
RT   agents.";
RL   J. Med. Chem. 56:8712-8735(2013).
RN   [3] {ECO:0007829|PDB:4MOT}
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.
RX   PubMed=24405701; DOI=10.1016/j.bmcl.2013.12.080;
RA   Kale R.R., Kale M.G., Waterson D., Raichurkar A., Hameed S.P.,
RA   Manjunatha M.R., Kishore Reddy B.K., Malolanarasimhan K., Shinde V.,
RA   Koushik K., Jena L.K., Menasinakai S., Humnabadkar V., Madhavapeddi P.,
RA   Basavarajappa H., Sharma S., Nandishaiah R., Mahesh Kumar K.N., Ganguly S.,
RA   Ahuja V., Gaonkar S., Naveen Kumar C.N., Ogg D., Boriack-Sjodin P.A.,
RA   Sambandamurthy V.K., de Sousa S.M., Ghorpade S.R.;
RT   "Thiazolopyridone ureas as DNA gyrase B inhibitors: optimization of
RT   antitubercular activity and efficacy.";
RL   Bioorg. Med. Chem. Lett. 24:870-879(2014).
RN   [4] {ECO:0007829|PDB:5BOC}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-226.
RA   Chen G.Y., Ng F.M., Tan Y.W., Poulsen A., Seetoh W., Lin G., Kang C.,
RA   Then S.W., Ahmad N.H., Wong Y.L., Ng H., Chia B.C.S., Lau Q.Y., Hill J.,
RA   Hung A.W., Keller T.H.;
RT   "Application of Fragment-based Drug Discovery against DNA GyraseB.";
RL   Submitted (MAY-2015) to the PDB data bank.
RN   [5] {ECO:0007829|PDB:5BOD}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-226.
RA   Chen G.Y., Ng F.M., Tan Y.W., Poulsen A., Seetoh W., Lin G., Kang C.,
RA   Then S.W., Ahmad N.H., Wong Y.L., Ng H.Q., Chia B.C.S., Lau Q.Y., Hill J.,
RA   Hung A.W., Keller T.H.;
RT   "Application of Fragment-based Drug Discovery against DNA GyraseB.";
RL   Submitted (MAY-2015) to the PDB data bank.
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC       relaxes supercoiled DNA. Performs the decatenation events required
CC       during the replication of a circular DNA molecule. {ECO:0000256|HAMAP-
CC       Rule:MF_00939}.
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_00939};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC       Rule:MF_00939}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00939}.
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DR   EMBL; AE007317; AAK99560.1; -; Genomic_DNA.
DR   PIR; D97966; D97966.
DR   RefSeq; NP_358350.1; NC_003098.1.
DR   RefSeq; WP_000037270.1; NC_003098.1.
DR   PDB; 4LP0; X-ray; 1.95 A; A=1-226.
DR   PDB; 4LPB; X-ray; 1.75 A; A=1-226.
DR   PDB; 4MOT; X-ray; 1.75 A; A=1-226.
DR   PDB; 5BOC; X-ray; 2.20 A; A=1-226.
DR   PDB; 5BOD; X-ray; 2.20 A; A=1-226.
DR   PDBsum; 4LP0; -.
DR   PDBsum; 4LPB; -.
DR   PDBsum; 4MOT; -.
DR   PDBsum; 5BOC; -.
DR   PDBsum; 5BOD; -.
DR   AlphaFoldDB; Q8DQB5; -.
DR   SMR; Q8DQB5; -.
DR   STRING; 171101.spr0756; -.
DR   KEGG; spr:spr0756; -.
DR   PATRIC; fig|171101.6.peg.836; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_1_2_9; -.
DR   Proteomes; UP000000586; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00939; ParE_type2; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005740; ParE_type2.
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   NCBIfam; TIGR01058; parE_Gpos; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF12; DNA TOPOISOMERASE 4 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4LP0, ECO:0007829|PDB:4LPB};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00939};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00939};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00939};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00939};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000586};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT   DOMAIN          427..541
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          391..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        391..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         78
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         118..124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         344
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            461
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            513
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            629
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ   SEQUENCE   647 AA;  71665 MW;  0AF7382C72772713 CRC64;
     MSKKEININN YNDDAIQVLE GLDAVRKRPG MYIGSTDGAG LHHLVWEIVD NAVDEALSGF
     GDRIDVTINK DGSLTVQDHG RGMPTGMHAM GIPTVEVIFT ILHAGGKFGQ GGYKTSGGLH
     GVGSSVVNAL SSWLEVEITR DGAVYKQRFE NGGKPVTTLK KIGTALKSKT GTKVTFMPDA
     TIFSTTDFKY NTISERLNES AFLLKNVTLS LTDKRTDEAI EFHYENGVQD FVSYLNEDKE
     ILTPVLYFEG EDNGFQVEVA LQYNDGFSDN ILSFVNNVRT KDGGTHETGL KSAITKVMND
     YARKTGLLKE KDKNLEGSDY REGLAAVLSI LVPEEHLQFE GQTKDKLGSP LARPVVDGIV
     ADKLTFFLME NGELASNLIR KAIKARDARE AARKARDESR NGKKNKKDKG LLSGKLTPAQ
     SKNPAKNELY LVEGDSAGGS AKQGRDRKFQ AILPLRGKVI NTAKAKMADI LKNEEINTMI
     YTIGAGVGAD FSIEDANYDK IIIMTDADTD GAHIQTLLLT FFYRYMRPLV EAGHVYIALP
     PLYKMSKGKG KKEEVAYAWT DGELEELRKQ FGKGATLQRY KGLGEMNADQ LWETTMNPET
     RTLIRVTIED LARAERRVNV LMGDKVEPRR KWIEDNVKFT LEEATVF
//