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Database: UniProt
Entry: A0A264Y9Z3_9BACT
LinkDB: A0A264Y9Z3_9BACT
Original site: A0A264Y9Z3_9BACT 
ID   A0A264Y9Z3_9BACT        Unreviewed;       649 AA.
AC   A0A264Y9Z3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=CHL74_02945 {ECO:0000313|EMBL:OZT04896.1};
OS   Prevotella sp. 885.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=2022527 {ECO:0000313|EMBL:OZT04896.1, ECO:0000313|Proteomes:UP000216632};
RN   [1] {ECO:0000313|EMBL:OZT04896.1, ECO:0000313|Proteomes:UP000216632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=885 {ECO:0000313|EMBL:OZT04896.1,
RC   ECO:0000313|Proteomes:UP000216632};
RA   Efimov B.A., Chaplin A.V., Kochetkova T.O., Sokolova S.R., Ogneva L.V.,
RA   Rebrikov D.V., Kondova I., Langermans J.A., Shkoporov A.N.;
RT   "Description of Prevotella sp. 885 sp. nov., isolated from rhesus macaque
RT   feces.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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:OZT04896.1}.
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DR   EMBL; NOVE01000004; OZT04896.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A264Y9Z3; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000216632; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd01030; TOPRIM_TopoIIA_like; 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   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; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 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; 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   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:OZT04896.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216632}.
FT   DOMAIN          411..521
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   649 AA;  74070 MW;  D371FF0CF84568EF CRC64;
     MEEEIQKPTV QYTDDNIRHL SDMEHVRTRP GMYIGRLGDG NLPEDGIYVL LKEVVDNSID
     EFKMNAGKRI EVDVEERKSV SVRDYGRGIP QGKLVEAVSM LNTGGKYDSK AFKKSVGLNG
     VGVKAVNALS SRFEVRSYRD GTVRALVFER GVLKSDVTEP TEDENGTYIF FQPDPTLFVG
     YSFHDDFVET MLRNYTYLNS GLTIMYNGRR IMSRNGLADL LTDTMTTEPL YPIIHMKGED
     IEIAFTHTDQ YGEEYHSFVN GQHTTQGGTH QSAFKEHIAR TIKEFFSKNY EFTDIRNGLV
     AAIAINVEEP MFESQTKIKL GSLQMAPGGE SINKYVGDFI KQEVDNYLHI HADVAEVMQQ
     KISSSEKERK AMAGVTKIAR ERAKKANLHN RKLRDCRIHY SDAKNDRKED SAIFITEGDS
     ASGSITKSRD VNTQAVFSLR GKPLNSYGLT KKVVYENEEF NLLQAALDIE DGLDTLRYNK
     VIVATDADVD GMHIRLLIIT FFLQFFPDLI KKGHVYVLQT PLFRVRNRRT KIKNKKVVAE
     ADARLTGKER KSDFITRYSY SEEERQQAIR DLGPDPEITR FKGLGEISPD EFAHFIGPDM
     RLEQVTLHKT DQVQKLLEYY MGKNTMERQN FIIDNLVVEE DLPEEEIIK
//
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