ID A0A498CL11_9FIRM Unreviewed; 661 AA.
AC A0A498CL11;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 08-NOV-2023, entry version 16.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=D4A47_10620 {ECO:0000313|EMBL:RLL09118.1};
OS Anaerotruncus massiliensis (ex Liu et al. 2021).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=2321404 {ECO:0000313|EMBL:RLL09118.1, ECO:0000313|Proteomes:UP000276301};
RN [1] {ECO:0000313|EMBL:RLL09118.1, ECO:0000313|Proteomes:UP000276301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22A2-44 {ECO:0000313|EMBL:RLL09118.1,
RC ECO:0000313|Proteomes:UP000276301};
RA Wang Y.-J.;
RT "Anaerotruncus faecis sp. nov., isolated from human feces.";
RL Submitted (OCT-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 -!- 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:RLL09118.1}.
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DR EMBL; RCHT01000022; RLL09118.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498CL11; -.
DR Proteomes; UP000276301; Unassembled WGS sequence.
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; 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; 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; 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:RLL09118.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000276301}.
FT DOMAIN 435..558
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 661 AA; 75724 MW; D5C04D20385211AF CRC64;
MPKKRTADYG NESISSLKGA DRVRKRPGVI FGSDGLEGCE HAMFEILSNS IDEAREGHGD
KILITRYRDQ SIEIEDFGRG IPVDYNQREE RYNWELVFCE LYAGGKYQTN EGESYEYSLG
LNGLGLCATQ YSSEYMDVEI YRDGFKYSLH FEHGENVGGL QKEETRRRAT GTKIRWRPDL
AVFTDIDIPL EYYADTIKRQ AVVNDGVTFL LRNQADSGFE ETEFRYENGI VDYVAELAGD
GTLTPIQFWK AERRGRDRED KPEYKVKLSV AFCFSNRVSR CEYYHNSSWL EHGGSPEKAV
KLAFTYMIDN YIKNAGKYQK GESKVTFADV EDCLVLVSSN FSTQTSYENQ TKKAITNKFV
YEAMNDFLRH QMEVYFIENP DEAARIAEQV LINKRSRENA EKTRLNLKKK LAGTVDMSNR
VQKFVDCRTK DVSRREIYIV EGDSALGACK LGRDSEFQAI IPVRGKILNC LKADYDKIFK
SDIIVDIFKV LGCGVEVTTK ANKDFSSFDL DGLRWNKIVI CTDADVDGFQ IRTLILTMLY
RLAPTLIEEG RVYIAESPLY EITTKDKTWF AYTEQEKTNA LEEIGNAKYT VQRSKGLGEN
EPDMMWLTTM NPETRRLIKV TPSQAKETSD MFDLLLGDNL AGRKEFIAEN GYQYLELADL
S
//
