ID D4MXQ0_ANAHA Unreviewed; 637 AA.
AC D4MXQ0;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=CL2_03050 {ECO:0000313|EMBL:CBL37395.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL37395.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL37395.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37395.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL37395.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL37395.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FP929061; CBL37395.1; -; Genomic_DNA.
DR RefSeq; WP_008392804.1; NC_021016.1.
DR AlphaFoldDB; D4MXQ0; -.
DR STRING; 649756.ERS852387_01237; -.
DR GeneID; 15230486; -.
DR KEGG; bprl:CL2_03050; -.
DR PATRIC; fig|245018.3.peg.98; -.
DR Proteomes; UP000008960; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 CDD; cd03366; TOPRIM_TopoIIA_GyrB; 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 InterPro; IPR034160; TOPRIM_GyrB.
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:CBL37395.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 419..537
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 637 AA; 70923 MW; 7F11A88A4FA62799 CRC64;
MANKTYDANS ISVLEGLEAV RKRPGMYIGS VSTKGLNHLI YEIVDNSVDE FLAGYCDEIT
VSLNKDGTAT ITDNGRGIPV GINERTGKTA VEMVFTMLHA GGKFGDGGYK ISGGLHGVGA
SVVNALSTWL TVTVKQGGKV YQQRYERGKI ITPLEVIGTC RKSDTGTNVQ FLPDPEIFDK
TYFKAAMVRN RLHETAYLNP KLTIHYVNER EGEETTVDYH EPEGICAYVK KLNEGKQMLH
EPVYFKRMID GIEAEVAFQY TEDFGENILG FCNNIYTIEG GTHITGFKTK FTTIMNQYAR
EIGVLKEKDS NFTGTDVRNG MTAIVSVKHP EPRFEGQTKT KLDNPDAAKA VGEIAGEELV
LYFDKNLDTL KKVLACAEKS AKIRKAEEKA KTNMLVKQKL SIDSNGKLAN CESRKAQDCE
IFIVEGDSAG GSAKTARNRK TQAILPIRGK ILNVEKATMD KVLANAEIKT MINAFGCGFS
EGYGNDFDIS KLRYHKIIIM TDADVDGAHI ATLLLTFFYR FMPELITHGH VFLATPPLYK
AMPQKGEETY LFDDAALTRY RAEHKGNFTL QRYKGLGEMD AQQLWETTLN PESRTLKQIE
IEDARMASDI TSMLMGSDVP PRRQFIYENA NEAMLDI
//
