ID   Q3HYJ3_STREE            Unreviewed;       820 AA.
AC   Q3HYJ3;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 92.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE   Flags: Fragment;
GN   Name=parC {ECO:0000313|EMBL:AAZ93278.1};
OS   Streptococcus pneumoniae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1313 {ECO:0000313|EMBL:AAZ93278.1};
RN   [1] {ECO:0000313|EMBL:AAZ93278.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=0.15GR00S {ECO:0000313|EMBL:AAZ93278.1};
RX   PubMed=16189113; DOI=10.1128/AAC.49.10.4315-4326.2005;
RA   Stanhope M.J., Walsh S.L., Becker J.A., Italia M.J., Ingraham K.A.,
RA   Gwynn M.N., Mathie T., Poupard J.A., Miller L.A., Brown J.R.,
RA   Amrine-Madsen H.;
RT   "Molecular evolution perspectives on intraspecific lateral DNA transfer of
RT   topoisomerase and gyrase loci in Streptococcus pneumoniae, with
RT   implications for fluoroquinolone resistance development and spread.";
RL   Antimicrob. Agents Chemother. 49:4315-4326(2005).
RN   [2] {ECO:0007829|PDB:2NOV}
RP   X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) OF 1-493.
RX   PubMed=17375187; DOI=10.1371/journal.pone.0000301;
RA   Laponogov I., Veselkov D.A., Sohi M.K., Pan X.S., Achari A., Yang C.,
RA   Ferrara J.D., Fisher L.M., Sanderson M.R.;
RT   "Breakage-reunion domain of Streptococcus pneumoniae topoisomerase IV:
RT   crystal structure of a gram-positive quinolone target.";
RL   PLoS ONE 2:E301-E301(2007).
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};
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DR   EMBL; DQ176455; AAZ93278.1; -; Genomic_DNA.
DR   PDB; 2NOV; X-ray; 2.67 A; A/B/C/D=1-487.
DR   PDBsum; 2NOV; -.
DR   AlphaFoldDB; Q3HYJ3; -.
DR   SMR; Q3HYJ3; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00187; TOP4c; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   HAMAP; MF_00937; ParC_type2; 1.
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   InterPro; IPR005741; TopoIV_A_Gpos.
DR   NCBIfam; TIGR01061; parC_Gpos; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   PANTHER; PTHR43493:SF9; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 5.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2NOV};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AAZ93278.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          4..457
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAZ93278.1"
SQ   SEQUENCE   820 AA;  92789 MW;  18D452B5041F82FD CRC64;
     IQNMSLEDIM GERFGRYSKY IIQDRALPDI RDGLKPVQRR ILYSMNKDSN TFDKSYRKSA
     KSVGNIMGNF HPHGDSSIYD AMVRMSQNWK NREILVEMHG NNGSMDGDPP AAMRYTEARL
     SEIAGYLLQD IEKKTVPFAW NFDDTEKEPT VLPAAFPNLL VNGSTGISAG YATDIPPHNL
     AEVIDAAVYM IDHPTAKIDK LMEFLPGPDF PTGAIIQGRD EIKKAYETGK GRVVVRSKTE
     IEKLKGGKEQ IVITEIPYEI NKANLVKKID DVRVNNKVAG IAEVRDESDR DGLRIAIELK
     KDANTELVLN YLFKYTDLQI NYNFNMVAID NFTPRQVGIV PILSSYIAHR REVILARSRF
     DKEKAEKRLH IVEGLIRVIS ILDEVIALIR ASENKADAKE NLKVSYDFTE EQAEAIVTLQ
     LYRLTNTDVV VLQEEEAELR EKIAMLAAII GDERTMYNLM KKELREVKKK FATPRLSSLE
     DTAKAIEIDT ASLIAEEDTY VSVTKAGYIK RTSPRSFAAS TLEEIGKRDD DRLIFVQSAK
     TTQHLLMFTS LGNVIYRPIH ELADIRWKDI GEHLSQTITN FETNEEILYV EVLDQFDDAT
     TYFAVTRLGQ IKRVERKEFT PWRTYRSKSV KYAKLKDDTD QIVAVAPIKL DDVVLVSQNG
     YALRFNIEEV PVVGAKAAGV KAMNLKEDDV LQSGFICNTS SFYLLTQRGS LKRVSIEEIL
     ATSRAKRGLQ VLRELKNKPH RVFLAGAVAE QGFVGDFFST EVDVNDQTLL VQSNKGTIYE
     SRLQDLNLSE RTSNGSFISD TISDEEVFDA YLQEVVTEDK
//