ID F4KNC1_PORAD Unreviewed; 673 AA.
AC F4KNC1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN OrderedLocusNames=Poras_1499 {ECO:0000313|EMBL:AEE13432.1};
OS Porphyromonas asaccharolytica (strain ATCC 25260 / DSM 20707 / BCRC 10618 /
OS JCM 6326 / LMG 13178 / VPI 4198) (Bacteroides asaccharolyticus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=879243 {ECO:0000313|EMBL:AEE13432.1, ECO:0000313|Proteomes:UP000006545};
RN [1] {ECO:0000313|Proteomes:UP000006545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25260 / DSM 20707 / VPI 4198
RC {ECO:0000313|Proteomes:UP000006545};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I., Lu M.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Porphyromonas asaccharolytica DSM 20707.";
RL Submitted (APR-2011) 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};
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DR EMBL; CP002689; AEE13432.1; -; Genomic_DNA.
DR RefSeq; WP_013760782.1; NC_015501.1.
DR AlphaFoldDB; F4KNC1; -.
DR STRING; 879243.Poras_1499; -.
DR KEGG; pah:Poras_1499; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_1_1_10; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000006545; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 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; 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:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 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; 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 Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Reference proteome {ECO:0000313|Proteomes:UP000006545}.
FT DOMAIN 434..544
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 561..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 673 AA; 75683 MW; 23B173782B583EA3 CRC64;
MPIQEPLNQP ELLDQATVAG YTEDDFRTLS WSEHIRKRPG MYIGKIGDGT QADDGIYILI
KEVIDNSIDE FVMGVGSEIR ITIDSETNEV QIRDYGRGIP LGKLVDATSK MNTGAKIDSQ
AFKKSVGLNG VGLKAVNALS STFTVQSWRE GETSSVTYER AEMVAHTPAA PCEDKGVHGT
LVSFTPDAEV FRNSHYDLRH VEALVRNYCY LNTGLTLYLN DKKYVSRHGL QDFLSDTITG
DPLYPIIRLT GPDIEVAITH IEQYGEEFYS FVNGQYTTQG GTHLTAFREQ VARVIKEFSG
KGFEYGDIRS GMAAAISIRI IEPEFESQTK IKLGSKEMVP QDPMFEHEPL RGVTVQKFVG
DFLKEKLDNY LHMHPDISEV MLQTIQANER ERKAMSGVTK LARERAKKAS LHNKKLRDCT
EHYNDPKAKN PELTSIFITE GNSASGSITQ SRDARYQAVF SLRGKPLNSY GLSKKVVYEN
EEFNLLQAAL NIEDGLEGLR YNRVIIATDA DDDGMHIRLL TLTFFLQFFP ELVRRGHVYI
LETPLYRVSL PAKRKKSITA RVASAGKKKG GKKATSEPAS ETETSAYCYS DQELNAAVER
MGASAQITRF KGLGEISANE FKELITEENI KLRQVSLRKE DNLKRMLHFY MGKNTPDRQD
FIIDNLIIDE EIV
//
