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Database: UniProt
Entry: Q4UKT4
LinkDB: Q4UKT4
Original site: Q4UKT4 
ID   PARE_RICFE              Reviewed;         662 AA.
AC   Q4UKT4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   01-OCT-2014, entry version 66.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000255|HAMAP-Rule:MF_00938};
DE            EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00938};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000255|HAMAP-Rule:MF_00938};
GN   Name=parE {ECO:0000255|HAMAP-Rule:MF_00938};
GN   OrderedLocusNames=RF_0988;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome
CC       segregation. It relaxes supercoiled DNA. Performs the decatenation
CC       events required during the replication of a circular DNA molecule.
CC       {ECO:0000255|HAMAP-Rule:MF_00938}.
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00938}.
CC   -!- COFACTOR: Magnesium. Binds two Mg(2+) per subunit. The magnesium
CC       ions form salt bridges with both the protein and the DNA. Can also
CC       accept other divalent metal cations, such as Mn(2+) and Ca(2+).
CC       {ECO:0000255|HAMAP-Rule:MF_00938}.
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE.
CC       {ECO:0000255|HAMAP-Rule:MF_00938}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type
CC       1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00938}.
CC   -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00938}.
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DR   EMBL; CP000053; AAY61839.1; -; Genomic_DNA.
DR   RefSeq; YP_247004.1; NC_007109.1.
DR   ProteinModelPortal; Q4UKT4; -.
DR   STRING; 315456.RF_0988; -.
DR   EnsemblBacteria; AAY61839; AAY61839; RF_0988.
DR   GeneID; 3400996; -.
DR   KEGG; rfe:RF_0988; -.
DR   PATRIC; 17892727; VBIRicFel64634_1181.
DR   eggNOG; COG0187; -.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02622; -.
DR   OMA; ICEEASK; -.
DR   OrthoDB; EOG6P334W; -.
DR   BioCyc; RFEL315456:GKEK-1017-MONOMER; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   HAMAP; MF_00938; ParE_type1; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_ATP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013759; Topo_IIA_cen_dom.
DR   InterPro; IPR013760; Topo_IIA_like_dom.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR005737; TopoIV_B_Gneg.
DR   InterPro; IPR006171; Toprim_domain.
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; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01055; parE_Gneg; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; DNA-binding; Isomerase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Topoisomerase.
FT   CHAIN         1    662       DNA topoisomerase 4 subunit B.
FT                                /FTId=PRO_0000273118.
FT   DOMAIN      439    553       Toprim. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
FT   NP_BIND     129    135       ATP. {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   METAL       445    445       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   METAL       518    518       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   METAL       518    518       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
FT   METAL       520    520       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
FT   BINDING      20     20       ATP. {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   BINDING      60     60       ATP. {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   BINDING      87     87       ATP. {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   BINDING     359    359       ATP. {ECO:0000255|HAMAP-Rule:MF_00938}.
FT   SITE        470    470       Interaction with DNA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        473    473       Interaction with DNA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        525    525       Interaction with DNA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
FT   SITE        641    641       Interaction with DNA. {ECO:0000255|HAMAP-
FT                                Rule:MF_00938}.
SQ   SEQUENCE   662 AA;  73954 MW;  7D80C19453C7F0D7 CRC64;
     MSDLFSFNKE KKNKLVDNNY SAKDIEVLEG LEPVRKRPGM YIGGTDSNAM HHLVSEVLDN
     AMDEAVAGFA SIITIKMHQD HSITIFDNGR GIPIDNHPKF PDKSALEVIL TTLHSGGKFS
     NNVYHTAGGL HGVGISVVNA LSKHLEIKVY KQGKLYSQSY SKGEKLTDLI CEEASKRLRG
     TSINFTPDPE IFSEKLHFNP KKIYELARSK AYLYRGVTIE WECEVEVPSD IPKKALINFP
     NGLKDYLSSK ITLDNLIIPE IFSGNIESTP DEIKLEWAIC WQNNDNSAFI QSYCNTVPTP
     QGGTHEQGLK SAILRGLKAY GEMIGNKKAA NLTIEDILET ASVVLSIFIA EPSFQGQTKE
     KLVSNGVSKP VENIIKDHFD HFLSSDKALA TNLLEHVIAI AEFRISKKNE KNISRKNATQ
     KLRLPGKLAD CTRTTPGGTE LFIVEGDSAG GSAKQARNRE TQAVLPLWGK VLNVASSTLE
     KIVNNQAIQD LEIALACGSL KNYKEENLRY EKIIIMTDAD VDGAHIASLL MTFFFLRMPK
     LVEEGHLYLA KPPLYRLTQS NKTYYAGDEE EKAKLTDKLS KASKAKIEVG RFKGLGEMMP
     AQLKETTMHP EKRSLLKVTL EDFQNVDKIV DDLMGKKPEK RFQFIYEQAL VKMDKIINEL
     DI
//
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