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Database: UniProt
Entry: A4SXA2_POLAQ
LinkDB: A4SXA2_POLAQ
Original site: A4SXA2_POLAQ 
ID   A4SXA2_POLAQ            Unreviewed;       662 AA.
AC   A4SXA2;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 109.
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   OrderedLocusNames=Pnuc_0900 {ECO:0000313|EMBL:ABP34116.1};
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153 {ECO:0000313|EMBL:ABP34116.1, ECO:0000313|Proteomes:UP000000231};
RN   [1] {ECO:0000313|EMBL:ABP34116.1, ECO:0000313|Proteomes:UP000000231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1
RC   {ECO:0000313|Proteomes:UP000000231};
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA   Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA   Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP34116.1; -; Genomic_DNA.
DR   RefSeq; WP_011902741.1; NC_009379.1.
DR   AlphaFoldDB; A4SXA2; -.
DR   GeneID; 31481266; -.
DR   KEGG; pnu:Pnuc_0900; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_1_0_4; -.
DR   OMA; NTWEVDG; -.
DR   Proteomes; UP000000231; 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: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   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   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   Reference proteome {ECO:0000313|Proteomes:UP000000231};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00938}.
FT   DOMAIN          431..544
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   BINDING         9
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         73
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         117..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            465
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            520
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            647
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ   SEQUENCE   662 AA;  72696 MW;  EA2C676194B52EC7 CRC64;
     MATRKTSEYS ESSIQVLKGL EPVRQRPGMY TRTDNPLHII QEVLDNASDE ALGGFGKHIT
     VTLHTDSSVS VEDDGRGIPV GIHPTEKLPV VEIVFTQLHA GGKFEKGTGG AYAFSGGLHG
     VGVSVTNALS KRLEVTVWRE GQVSTLTFAD GKVIEKLKTR ASSKEDKSHG TRVRAWPDSK
     YFDSAAIPMP ELIRLLRSKA VLLPGVKVTL IQEKSGDSQT WQYAQGLRGY LNEAIAQAGH
     GPEVIPPFEG EQYATGNGED DSFAEGEGAA WVVSWTEDGA PVRESYVNLI PTPAGGTHES
     GLREGLFNAV KGFIEMHALQ PKGVKLMPED VFARASFILS AKVLDPQFQG QIKERLNSRD
     AVRLVSGYAK SALELWLNQH VDYGRKLADL VIKQAQARTR AGQKVEKKKS SGVAVLPGKL
     TDCESEDIAQ NEIFLVEGDS AGGSAKMGRN KEYQAILPLR GKVLNTWEAE RDRLFANNEV
     HDIAVAIGVD PHGLNDTPDL SNLRYGKVCI LSDADVDGAH IQVLLLTLFY KHFPKLIDLG
     HIYISRPPLF RVDAPARGKK PAQKIYALDA SELQAIEDKL RKDGVKETAW QISRFKGLGE
     MSAEQLWDTT LNPDTRRLLP VTLGAWTEDE TFKTMDMLMG KSESGARRDW LEERGNEVEA
     DI
//
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