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Database: UniProt
Entry: A0A0R1X8Z4_9LACO
LinkDB: A0A0R1X8Z4_9LACO
Original site: A0A0R1X8Z4_9LACO 
ID   A0A0R1X8Z4_9LACO        Unreviewed;       658 AA.
AC   A0A0R1X8Z4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00939};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00939};
GN   Name=parE {ECO:0000256|HAMAP-Rule:MF_00939};
GN   ORFNames=FD32_GL001103 {ECO:0000313|EMBL:KRM24980.1};
OS   Limosilactobacillus panis DSM 6035.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=1423782 {ECO:0000313|EMBL:KRM24980.1, ECO:0000313|Proteomes:UP000051412};
RN   [1] {ECO:0000313|EMBL:KRM24980.1, ECO:0000313|Proteomes:UP000051412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6035 {ECO:0000313|EMBL:KRM24980.1,
RC   ECO:0000313|Proteomes:UP000051412};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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_00939}.
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_00939};
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_00939}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00939}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRM24980.1}.
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DR   EMBL; AZGM01000140; KRM24980.1; -; Genomic_DNA.
DR   RefSeq; WP_047770085.1; NZ_LDPB01000145.1.
DR   AlphaFoldDB; A0A0R1X8Z4; -.
DR   STRING; 1423782.FD32_GL001103; -.
DR   PATRIC; fig|1423782.4.peg.1154; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000051412; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_00939; ParE_type2; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005740; ParE_type2.
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; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   NCBIfam; TIGR01058; parE_Gpos; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF12; 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; PR01159; DNAGYRASEB.
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_00939};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00939};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00939};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00939};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051412};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_00939}.
FT   DOMAIN          426..540
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          388..419
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         8
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         48
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         116..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   BINDING         343
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            460
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            512
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
FT   SITE            628
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00939"
SQ   SEQUENCE   658 AA;  73391 MW;  E9B7B9103E9E0522 CRC64;
     MTTKKVKYDE SSIQVLKGLE AVRKRPGMYI GSTDARGLHH LVYEIVDNAV DEALSGYGDE
     IKVTIEADNS ITVQDHGRGM PVGMHASGKP TPEVIMTVLH AGGKFGQADG YKTSGGLHGV
     GASVVNALST NLTLTIVRDH VRYQEKFKNG GQPVGTLKKL GKTREQSGTT VSFKPDPAIF
     TTTVYDYNTL ANRLRESAFL LKGIKIVLTD KRAGQERQDV FQYKDGIQEF VSYLNEGKDT
     LGKIMYFDGK DQGVEVEVAA QYNDGYSETL LSFVNNVRTP DGGTHEAGFR SAWTKTFNEY
     AKRVGLLKNN DKNLEGSDVR EGLTAVISVR IPERLLQFEG QTKDKLGTPE ARKIVDTIVS
     EQLNYALMEN GDFAQMLIRK SLKAREAREA ARKARNQARG GKRKSRKERN LSGKLTPAQS
     KNAQKNELFL VEGDSAGGSA KQGRDRKFQA ILPLRGKVLN TEKAKLDDVL KNEELNTIIY
     TVGAGAGSEF DVKDANYDKI IIMTDADDDG AHIQILLLTF FYKYMRPMIE AGKIYIALPP
     LYRLQQGRGA KTKITYAWTN EELTKLTKRM GKTAQLQRFK GLGEMNADQL WETTMNPATR
     TLIRVRIEDA ELAERRVTTL MGNKVEPRRE WIENNVQFTL SDDQESDKLV ASKKHLNK
//
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