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Database: UniProt
Entry: A9NF71_ACHLI
LinkDB: A9NF71_ACHLI
Original site: A9NF71_ACHLI 
ID   A9NF71_ACHLI            Unreviewed;       651 AA.
AC   A9NF71;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   Name=parE {ECO:0000313|EMBL:ABX81001.1};
GN   OrderedLocusNames=ACL_0379 {ECO:0000313|EMBL:ABX81001.1};
OS   Acholeplasma laidlawii (strain PG-8A).
OC   Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Acholeplasma.
OX   NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX81001.1, ECO:0000313|Proteomes:UP000008558};
RN   [1] {ECO:0000313|EMBL:ABX81001.1, ECO:0000313|Proteomes:UP000008558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-8A {ECO:0000313|EMBL:ABX81001.1,
RC   ECO:0000313|Proteomes:UP000008558};
RX   PubMed=21784942; DOI=10.1128/JB.05059-11;
RA   Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA   Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA   Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA   Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA   Ladygina V.G., Govorun V.M.;
RT   "Complete genome and proteome of Acholeplasma laidlawii.";
RL   J. Bacteriol. 193:4943-4953(2011).
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};
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DR   EMBL; CP000896; ABX81001.1; -; Genomic_DNA.
DR   RefSeq; WP_012242332.1; NC_010163.1.
DR   AlphaFoldDB; A9NF71; -.
DR   STRING; 441768.ACL_0379; -.
DR   GeneID; 66293375; -.
DR   KEGG; acl:ACL_0379; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_1_2_14; -.
DR   OMA; KIAYAWT; -.
DR   OrthoDB; 9802808at2; -.
DR   Proteomes; UP000008558; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
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   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   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABX81001.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008558}.
FT   DOMAIN          426..540
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   651 AA;  73014 MW;  67D82F8411E44B8C CRC64;
     MAKTNYDETS IQILEGLEAV RKRPGMYIGS TDHRGLHHLV WEIVDNAMDE VLAGFGSEIT
     VTIKPDNAIE VLDDGRGMPY KKHTSGVPTT QVIFTVLHAG GKFGGDGAYK VAGGLHGVGS
     SVVNALSSVL EVTVYKDGGI FRQRFENGGK KIFNQEKIGD TKKTGTQVYF KPDPSIFSTT
     LYNYDTIKER LKESAYLIKG LKINLIDERN NKKETFKFDE GIKAYVEFMN TGKNALHDVT
     DVEGTFNTAK DSAIEVEVAL QYTDSYSENI ISFVNNVRTK DGGTHEIGFK SALTKVINDY
     ARKYNHIKEK DSNIDGVDIR EGLTAIVSLR IPETVLEFEG QTKGKLGTPE ARNALETVFY
     EKFNTFLEEN SDAALSIITK AVAAANAREA ARKAREEARA GKKRSKKEVI LSGKLTPAQG
     KDKSINELFL VEGDSAGGSA KQGRNRRFQA ILPLRGKVIN TERTNTETIL KNEEISTMIY
     TIGADFGEDF DIKKCNYNKV IIMTDADDDG AHIQTLLLTF FFRYMRPLIE AGRLYIAQPP
     FYKVTYKKNK KEETVYAWSD EDLKETLESI GQNYMITRFK GLGEMNFYQL WETTMNPESR
     TLIQVTIDDL NVSDKHISVL MGDQVAPRRE WIEANVDFEV TDEFDIEGKV R
//
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