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Database: UniProt
Entry: A0A0C3I4Y0_9VIBR
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ID   A0A0C3I4Y0_9VIBR        Unreviewed;       626 AA.
AC   A0A0C3I4Y0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 47.
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   ORFNames=SU60_19065 {ECO:0000313|EMBL:KIN09407.1};
OS   Vibrio mytili.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=50718 {ECO:0000313|EMBL:KIN09407.1, ECO:0000313|Proteomes:UP000031977};
RN   [1] {ECO:0000313|EMBL:KIN09407.1, ECO:0000313|Proteomes:UP000031977}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CAIM 528 {ECO:0000313|EMBL:KIN09407.1,
RC   ECO:0000313|Proteomes:UP000031977};
RA   Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra J.;
RT   "Draft genome of Vibrio mytili type strain CAIM 528.";
RL   Submitted (JAN-2015) 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}.
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:KIN09407.1}.
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DR   EMBL; JXOK01000081; KIN09407.1; -; Genomic_DNA.
DR   RefSeq; WP_041156904.1; NZ_JXOK01000081.1.
DR   AlphaFoldDB; A0A0C3I4Y0; -.
DR   STRING; 50718.SU60_19065; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000031977; 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: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; 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; 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   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         5
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         110..116
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            613
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ   SEQUENCE   626 AA;  69317 MW;  5FBF8F0E846EEF4B CRC64;
     MTEQYNAGAI EVLNGLEPVR RRPGMYTDTA RPNHLGQEVI DNSVDEALAG HASKVQVILH
     ADQSLEVIDD GRGMPVDIHP EEKVSGVELI LCKLHAGGKF SNKNYQFSGG LHGVGISVVN
     ALSKRVEVTV RRDGQVYEIA FEHGDKVSDL TVTGTCGRRN RGTSVHFWPD TKYFDSGNFS
     VTRLVNNLRA KAVLCPGLEI TLTDKVNGKD YKWYYEDGLK DYLAEGVKGY PVIPEAPFTG
     EFLAETEAAN WAVIWQPEGG EMITESYVNL IPTAQGGTHV NGLRQGLLDA MREFCEFRNL
     LPRGVKLTGD DVFDRCSYVL SVKIQDPQFA GQTKERLSSR QTAAFVSGVV KDAFSLWLNE
     KPQLAEQLAE VCIANAHRRM RAAKKVVRKK VASGPALPGK LTDCSVQDLS RTEIFFVEGD
     SAGGSAKQAR DREFQAVMPL RGKILNTWEV SADQVLASQE VHDISVALGI DPDNDNLDGL
     RYGKICILAD ADSDGLHIAT LLCALFTRHF RALVEAGHIY VAMPPLYRID CGKEVFYALD
     DDEKDGILER LSKKKAKINV QRFKGLGEMN PLQLRETTMD PNTRRLVQLT IDDSVATMEM
     MDMLLGKKRA DDRRSWLQSN GDLAEV
//
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