ID D1PMH3_9FIRM Unreviewed; 659 AA.
AC D1PMH3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=SUBVAR_05533 {ECO:0000313|EMBL:EFB75758.1};
OS Subdoligranulum variabile DSM 15176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=411471 {ECO:0000313|EMBL:EFB75758.1, ECO:0000313|Proteomes:UP000003438};
RN [1] {ECO:0000313|EMBL:EFB75758.1, ECO:0000313|Proteomes:UP000003438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15176 {ECO:0000313|EMBL:EFB75758.1,
RC ECO:0000313|Proteomes:UP000003438};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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 -!- 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:EFB75758.1}.
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DR EMBL; ACBY02000023; EFB75758.1; -; Genomic_DNA.
DR RefSeq; WP_007046918.1; NZ_GG704769.1.
DR AlphaFoldDB; D1PMH3; -.
DR STRING; 411471.SUBVAR_05533; -.
DR GeneID; 78305738; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_1_2_9; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000003438; 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: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; 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; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003438};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 433..556
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 659 AA; 74760 MW; 18499B4F6D24F83C CRC64;
MAKKQQEYGN DSIRQLKGAD RVRKRPAVIF GSDGVEGCAH SIFEIISNSI DEARDGYGNR
INVTLFPDHV VEVEDFGRGI PVDYNKAEQR WNWDLVFCEL YAGGKYAEGG GNYDFSLGLN
GLGLCATQYA SEWMTADIYR DGFHYHLDFQ KGENVGGLQK EEYKGRRTGS VIRWKPDTEV
FTDIAVPPET FQDMLRRQAV VNDGVTLVFT DKSGKDTQKY EYLYEHGIAD YANEIVGDEA
LTPVHFCSGA AVGRDRADQP DYQVRMNVAF AFSNTVQTLE YYHNSSWLEH GGSPDRAVRS
AFVSQINAWL KSKGLYKKNE SAITFSDVQD CLVLVSSSFS TRTSYENQTK KAITNKFVAQ
AMTEFLKHQL EVYFIEHPDE AEKACKQVLI NKQSREHAEK ARITIKKTMT QQMDLANRVQ
KFVDCRTKDA SRRELYIVEG DSAMGAVKQS RDSEFQAIMP IRGKILNCLK ADYARIFKSD
IITDLIRVMG CGVELGGSHN KDLASFNLDN LRFNKVVICT DADVDGYQIR TLVLTMLYRL
TPTLINKGYV YIAESPLYEI NTKNKTYFAY TEPEKADILR RIEGEKYTIQ RSKGLGENDP
EMMWLTTMSP ESRRLIKVLP TDAERTAQVF DLLLGDNLQG RKEHIAEHGA EYLDDLDVS
//