ID A0A2K4ZNE9_9FIRM Unreviewed; 702 AA.
AC A0A2K4ZNE9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN Name=topB_4 {ECO:0000313|EMBL:SOY32009.1};
GN ORFNames=AMURIS_04762 {ECO:0000313|EMBL:SOY32009.1};
OS Acetatifactor muris.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetatifactor.
OX NCBI_TaxID=879566 {ECO:0000313|EMBL:SOY32009.1, ECO:0000313|Proteomes:UP000236311};
RN [1] {ECO:0000313|EMBL:SOY32009.1, ECO:0000313|Proteomes:UP000236311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP69 {ECO:0000313|EMBL:SOY32009.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000213};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446}.
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DR EMBL; OFSM01000036; SOY32009.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4ZNE9; -.
DR OrthoDB; 9803554at2; -.
DR Proteomes; UP000236311; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR013825; Topo_IA_cen_sub2.
DR InterPro; IPR013826; Topo_IA_cen_sub3.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR InterPro; IPR005738; TopoIII.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR NCBIfam; TIGR01056; topB; 1.
DR PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SOY32009.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236311};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 1..134
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 702 AA; 77177 MW; EE23F802F3321F5D CRC64;
MKLVIAEKPS VAMSLAAVLG ANEKKDGYLE GGGYLVSWCV GHLLELAQPE AYGEQYARWR
YGDLPILPEE WKYEVPKDKK KQLGLLCRLM KDKRVESVVC ATDAGREGEL IFRLVYGHAG
CRKPMERLWI SSMEDAAIRD GFEHLRPGSD YDKLYDAAVC RAGADWLIGI NATRLFSVLY
GVTLNVGRVM SPTLALLVQR EADIEAFASR PFYVPEITCG GFTASGEKLP DKAGAEKIRM
ESDGQAASVL SVEKQVKTVQ PPRLYDLTTL QRECNRIYGY TAQQTLDYVQ SLYEKKLATY
PRTDSQFLTE DMQATAASLI LWLRDNMPFG KGCAGEPDIG RVTDSGKVTD HHAIIPTAEI
ARTDLSGLPS GERDVLTLIA ARLLCATAQA HRFEAVAAVL DCRGHSFTAK GKTVLQAGWK
EVERLYRMGL KEPRPEDDGN TDASLPMLQE GQVFETASAS IREGRTSPPK HYTEDSLLAA
METAGAGDMP EDAERKGLGT PATRAAILEK LVSAGFVERR KKQLIPTEKG TNLILVLPDN
IKSPVLTAEW ESMLKQVERG ELAADAFMGQ IADMSRALVK EHTAPEECFA GLFPDAKRNG
REAVGACPRC GASVYEGKKG FFCDNRDCSF ALWKDNKFFS GKKKSITKPV AAALLKEGRV
SMSGLYSEKT GKTYDAVVLL DDTGGKYVNF RLEFPAKKGR GK
//
