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Database: UniProt
Entry: A1EGQ0_9BACT
LinkDB: A1EGQ0_9BACT
Original site: A1EGQ0_9BACT 
ID   A1EGQ0_9BACT            Unreviewed;       424 AA.
AC   A1EGQ0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-NOV-2023, entry version 57.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE   Flags: Fragment;
GN   Name=gyrB {ECO:0000313|EMBL:ABL67990.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:ABL67990.1};
RN   [1] {ECO:0000313|EMBL:ABL67990.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wan M., Zhang F., Yin H., Yang Y., Qiu G.;
RT   "GyrB sequences of Acidithiobacillus ferrooxidans and clones in acid mine
RT   drainage.";
RL   Submitted (NOV-2006) 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};
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DR   EMBL; EF124834; ABL67990.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1EGQ0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 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   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; 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   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; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
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   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT   DOMAIN          333..424
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABL67990.1"
FT   NON_TER         424
FT                   /evidence="ECO:0000313|EMBL:ABL67990.1"
SQ   SEQUENCE   424 AA;  46600 MW;  C68069BAE59AAD89 CRC64;
     EVIMTVLHAG GKFGGKVYDT SGGLHGVGSS VVNALSEWLE VEVARERQNH VMRFERGKPA
     GKLKNTGSVN RRGTIVRFKP DAQIFGSEAH FSPAMLYRMA KSKAYLFRGV EIHWRCDPGL
     IRNGKTPADE ILKFPGGLAD FLRSEIEGET TVSPRLFLGR TENKDGKGAV EWAVAWAPER
     DGFMQSFCNT IPTPLGGTHE QGLRNALTKA LRAYGERAGN KKTAQITPDD VMSAACAVLS
     VFIREPEFQG QTKEKLSTQD AQRLVETVVR DHFDHWLAES PAEADRLLSF VIDQADDRLK
     RRQDRETQRK SATRKLLLPG KLTDCTRDAP GGTELFLVEG DSAGGSAKQA RDRTTQAVLP
     LRGKILNVAS AAAGKLAQNQ ELSDLLLALG CGAGSKYREE ELRYERVIIM TDADVDGSHI
     RTLL
//
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