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Database: UniProt
Entry: A0A3B7M3J9_9GAMM
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ID   A0A3B7M3J9_9GAMM        Unreviewed;       626 AA.
AC   A0A3B7M3J9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00938};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
GN   Name=parE {ECO:0000256|HAMAP-Rule:MF_00938,
GN   ECO:0000313|EMBL:AXY58744.1};
GN   ORFNames=CDG61_01015 {ECO:0000313|EMBL:AXY58744.1};
OS   Acinetobacter sp. WCHAc010052.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=2004647 {ECO:0000313|EMBL:AXY58744.1, ECO:0000313|Proteomes:UP000264387};
RN   [1] {ECO:0000313|EMBL:AXY58744.1, ECO:0000313|Proteomes:UP000264387}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHAc010052 {ECO:0000313|EMBL:AXY58744.1,
RC   ECO:0000313|Proteomes:UP000264387};
RA   Hu Y., Long H., Feng Y., Zong Z.;
RT   "The complete genome of Acinetobacter sp. strain WCHAc010052.";
RL   Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
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_00938}.
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_00938};
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_00938}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00938}.
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DR   EMBL; CP032143; AXY58744.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7M3J9; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000264387; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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: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_00938; ParE_type1; 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; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR005737; TopoIV_B_Gneg.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   NCBIfam; TIGR01055; parE_Gneg; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF4; 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; PR01098; TOPISMRASE4B.
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|HAMAP-Rule:MF_00938};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00938};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00938}.
FT   DOMAIN          412..525
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   BINDING         4
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         41
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         109..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            446
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            497
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            611
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ   SEQUENCE   626 AA;  68929 MW;  1938263982CB3B1B CRC64;
     MSQYTAQSLE VLSGLDPVRR RPGMYTDTSR PNHLAQEVID NSVDEALAGH ASKITVTVYK
     DGSLSVEDNG RGMPVDIHPE YGQSGIEIIL TKLHAGGKFS TDNYQFSGGL HGVGISVVNA
     LSDRVEVEVQ RQGNLYKMAF EHGEAVAPLE VLEGKAPKRA SGTTVHFWPE AKYFDSPKFA
     LKALKHNLKA KAVLAAGLQI IYIDQINDEK IEWQFENGLV DYLMDELQDR DIVPEPAFVA
     TGEAERASAE FAICWNVEGG EQIQESYVNL IPTAQGGTHV NGLRSGVTDA MREFCELRNL
     LPRNMKLSAE DVWDGVNYIL SLKFQEPQFS GQTKERLSSR EASSIVLNIA KDAFALWLNQ
     NSDVAMQLAE MVIAKAGRRL KAAKKVERKK IVAGPTLPGK LSDCVGHTLE ESELFIVEGD
     SAGGSAKQAR DKNFQAIMPI RGKILNTWEV SSDEVLASQE VHNIAIAIGV DPGSDDLSEL
     RYGKICILAD ADSDGLHIAT LLCALFVKHF PAMVDAGHLY VAMPPLFRID DAKDVHYALD
     EQELEAILKK VKTKNPQITR FKGLGEMNAS QLRETTLDPN TRRLVQLDLD DTQLTANLLD
     KLLAKKRSGD RKDWLEQKGN LADLGV
//
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