ID   A0A1R3SV23_9BACT        Unreviewed;       910 AA.
AC   A0A1R3SV23;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=DNA topoisomerase IV subunit A {ECO:0000313|EMBL:SCD20163.1};
GN   ORFNames=PSM36_1340 {ECO:0000313|EMBL:SCD20163.1};
OS   Proteiniphilum saccharofermentans.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae;
OC   Proteiniphilum.
OX   NCBI_TaxID=1642647 {ECO:0000313|EMBL:SCD20163.1, ECO:0000313|Proteomes:UP000187464};
RN   [1] {ECO:0000313|EMBL:SCD20163.1, ECO:0000313|Proteomes:UP000187464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M3/6 {ECO:0000313|EMBL:SCD20163.1};
RA   Seilhamer J.J.;
RL   Submitted (AUG-2016) 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 GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
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; LT605205; SCD20163.1; -; Genomic_DNA.
DR   RefSeq; WP_076930003.1; NZ_LT605205.1.
DR   AlphaFoldDB; A0A1R3SV23; -.
DR   STRING; 1642647.PSM36_1340; -.
DR   KEGG; psac:PSM36_1340; -.
DR   Proteomes; UP000187464; Chromosome i.
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:0006265; P:DNA topological change; IEA:InterPro.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SCD20163.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187464};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          45..481
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..898
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   910 AA;  103887 MW;  8343F4480F903D92 CRC64;
     MSPKLPNDDD ITEREENMEE DEALLSSESF SGSKVPVRLG DDSSLNLSKM YQNWFLDYAS
     YVILERAVPH ISDGLKPVQR RILHAMKRMD DGRYNKVANI IGTTMQYHPH GDASIGDALV
     QLGQKDLLID CQGNWGNILT GDGAAAPRYI EARLNKFALE VLFDPKTTEW KASYDGRNKE
     PVTLPAKFPL LLVQGAEGIA VGLSSKILPH NFNEVCDAAV SYLQEEEFTL YPDFQTGGYI
     DVEKYNDGER GGSVKIRTTI SKIDNKTLVI KDIPYGKTTA GLVDSILKAN EKGKIKIKKV
     DDITAQNVEI HVQLAPGVSS DKTIDALYAF TDCEISISPN CCVIDDNRPH FLTVSDVLRS
     SVDTTRELLR RELEIEKSEK QEALLFASLE KIFIEERIYK DKEFENAKNM DIAVMHIDQR
     LEPYKPSFLR EITRDDILRL MEIRMGRILK FNSDKSDELI AKLKEEIGEI DHNLNHLVDY
     TIAWFLMLKE KYGKNFPRRT IIRSFENIEA TKVVEANEKL YINREEGFIG TGMKKDEFVC
     NCSDIDDIIV FFKDGKYKVV KVSDKMFVGK GILYAGVFKR NDKRTIYNVV YRDGKKAPHY
     IKRFAVTGIT RDKEYDLTRG KAGSRIAYFS VNPNGEAETI RVILKPKPRM RILQFEKDFS
     EIEIKGRQAM GNILTKAEVH RIQLKQKGVS TLGGRKVWFD PDVFRLNYEG SGKFLGEFQG
     DDMILVVTTD GEYYICNFDL TNHFPHNILH IGKYDEHKVW TAALFDADQG YAYLKRFTFE
     PSEKPLRFVG DNTDSRLFLL TDAVYPRVKA VFGGHDDFRE PLEIDVEEFI GVKSYKAKGK
     RISNYEVTEV EELEPLRFPE PEEEPQQTMK VEITEENGDN GENGENGENV DEDISDADLR
     DEITGQMKLF
//