ID A0A2P8GZP8_9MICO Unreviewed; 708 AA.
AC A0A2P8GZP8;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=CLV49_3064 {ECO:0000313|EMBL:PSL39428.1};
OS Labedella gwakjiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=390269 {ECO:0000313|EMBL:PSL39428.1, ECO:0000313|Proteomes:UP000241203};
RN [1] {ECO:0000313|EMBL:PSL39428.1, ECO:0000313|Proteomes:UP000241203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21548 {ECO:0000313|EMBL:PSL39428.1,
RC ECO:0000313|Proteomes:UP000241203};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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:PSL39428.1}.
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DR EMBL; PYAU01000001; PSL39428.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8GZP8; -.
DR Proteomes; UP000241203; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
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; 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:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE 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|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PSL39428.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000241203};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 481..595
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 708 AA; 77045 MW; CCEAAECE711496FB CRC64;
MFGAAGELVW VSVTDYSARH LSVLEGLEAV RKRPGMYIGT TDSRGLMHCL WEIIDNSVDE
ALAGNGSQIG IVLHPDDSVE VRDTGRGIPV DIEPKTGLSG VEVVFTKLHA GGKFGSGSYA
ASGGLHGVGA SVVNALSERL DVEVDRNGKT WAMSFHRGEP GIFDDSAGRT PDAPFTPFEK
GSVLRSVGKV AKGVTGTRVR YWADRQIFTP GATFNVDDLH ARARQTAFLV PGLGIRIDDE
RATEATGEGA SVSEFRYDGG ISEYVDFLSN DAPVTDTWRL TGDGTFSETV PVLQDSGAMV
PTEIERTCSV DVALRWGSGY DTAVRSYVNI ISTPKGGTHQ SGFEQGLIKV VRSQVEQNAR
RLKVGNDKLE KDDVMAGLTA VVTVRVPEPQ FEGQTKEVLG TPAVRAIVAS VVGERLKERF
ASTKREDKAQ TALVLDKVVA EMKTRISARA HKETQRRKNA LESSTLPAKL VDCRSSDVAS
TELFIVEGDS ALGTAKLARN SEFQALLPIR GKILNVQKAS VSDMLSNTEC ASILQVIGAG
SGRTFDLEAA RYGKVILMSD ADVDGAHIRT LLLTLFFRYM RPLIEAGRVF AAVPPLHRVV
VVNPGSKPND IIYTYSEQEL QGVLTGLKRS NKRYQEPIQR YKGLGEMDAE QLASTTMERA
HRTLRRVRIE DAEMAGNVFE LLMGNDVAPR KEFIIDSSDR LSRDRIDV
//
