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-MAY-2013, entry version 58.
DE RecName: Full=DNA topoisomerase 4 subunit B;
DE EC=5.99.1.3;
DE AltName: Full=Topoisomerase IV subunit B;
GN Name=parE; 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 (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC of double-stranded DNA.
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+) (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE (By similarity).
CC -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type
CC 1 subfamily.
CC -!- SIMILARITY: Contains 1 Toprim domain.
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DR EMBL; CP000053; AAY61839.1; -; Genomic_DNA.
DR RefSeq; YP_247004.1; NC_007109.1.
DR HSSP; P20083; 1S14.
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; QARDKEF; -.
DR ProtClustDB; PRK05559; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR SUPFAM; SSF56719; Topo_IIA_cen; 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.
FT NP_BIND 129 135 ATP (By similarity).
FT METAL 445 445 Magnesium 1; catalytic (By similarity).
FT METAL 518 518 Magnesium 1; catalytic (By similarity).
FT METAL 518 518 Magnesium 2 (By similarity).
FT METAL 520 520 Magnesium 2 (By similarity).
FT BINDING 20 20 ATP (By similarity).
FT BINDING 60 60 ATP (By similarity).
FT BINDING 87 87 ATP (By similarity).
FT BINDING 359 359 ATP (By similarity).
FT SITE 470 470 Interaction with DNA (By similarity).
FT SITE 473 473 Interaction with DNA (By similarity).
FT SITE 525 525 Interaction with DNA (By similarity).
FT SITE 641 641 Interaction with DNA (By similarity).
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
//
