TOP1_SYNE7
ID TOP1_SYNE7 Reviewed; 883 AA.
AC P34185; Q31NC3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE EC=5.6.2.1 {ECO:0000255|HAMAP-Rule:MF_00952};
DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952};
DE AltName: Full=Omega-protein;
DE AltName: Full=Relaxing enzyme;
DE AltName: Full=Swivelase;
DE AltName: Full=Untwisting enzyme;
GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952};
GN OrderedLocusNames=Synpcc7942_1416;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7659748; DOI=10.1104/pp.108.4.1461;
RA Ronen-Tarazi M., Lieman-Hurwitz J., Gabay C., Orus M.I., Kaplan A.;
RT "The genomic region of rbcLS in Synechococcus sp. PCC 7942 contains genes
RT involved in the ability to grow under low CO2 concentration and in
RT chlorophyll biosynthesis.";
RL Plant Physiol. 108:1461-1469(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC is introduced during the DNA replication and transcription, by
CC transiently cleaving and rejoining one strand of the DNA duplex.
CC Introduces a single-strand break via transesterification at a target
CC site in duplex DNA. The scissile phosphodiester is attacked by the
CC catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC DNA strand. The free DNA strand then undergoes passage around the
CC unbroken strand, thus removing DNA supercoils. Finally, in the
CC religation step, the DNA 3'-OH attacks the covalent intermediate to
CC expel the active-site tyrosine and restore the DNA phosphodiester
CC backbone. {ECO:0000255|HAMAP-Rule:MF_00952}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00952};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00952};
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00952}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51086.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X72391; CAA51086.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CP000100; ABB57446.1; -; Genomic_DNA.
DR PIR; S32158; S32158.
DR RefSeq; WP_011242453.1; NC_007604.1.
DR AlphaFoldDB; P34185; -.
DR SMR; P34185; -.
DR STRING; 1140.Synpcc7942_1416; -.
DR PRIDE; P34185; -.
DR EnsemblBacteria; ABB57446; ABB57446; Synpcc7942_1416.
DR KEGG; syf:Synpcc7942_1416; -.
DR eggNOG; COG0550; Bacteria.
DR HOGENOM; CLU_002929_2_0_3; -.
DR OMA; YAQPKQR; -.
DR OrthoDB; 223233at2; -.
DR BioCyc; SYNEL:SYNPCC7942_1416-MON; -.
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-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR CDD; cd00186; TOP1Ac; 1.
DR CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 1.
DR HAMAP; MF_00952; Topoisom_1_prok; 1.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR023406; Topo_IA_AS.
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; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR PANTHER; PTHR42785; PTHR42785; 2.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 4.
DR PRINTS; PR00417; PRTPISMRASEI.
DR SMART; SM00437; TOP1Ac; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56712; SSF56712; 1.
DR TIGRFAMs; TIGR01051; topA_bact; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding; Isomerase; Magnesium; Metal-binding; Topoisomerase.
FT CHAIN 1..883
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145167"
FT DOMAIN 2..126
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT REGION 175..180
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT REGION 271..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 320
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 32
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 151
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 152
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 155
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 160
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 167
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 322
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT SITE 515
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00952"
FT CONFLICT 101..102
FT /note="ES -> KV (in Ref. 1; CAA51086)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="L -> V (in Ref. 1; CAA51086)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 883 AA; 98296 MW; C90DAC6EE1202B9A CRC64;
MPKLVIVESP TKARTIRNYL PKDYRVEASM GHVRDLPQSA SDIPTELKGE KWSNLGVDVE
NNFAPLYIVP KDKKKIVKTL KDALKDADEL ILATDEDREG ESISWHLLQL LQPRVPTKRM
VFHEITQEAI QAALKNCRDV DQRLVHAQET RRILDRLVGY TLSPLLWKKI AWGLSAGRVQ
SVAVRLLVQR ERARRAFRQG SYWDLKAQLT VEAGQFEAKL WTLAGQRLAT GNDFDESTGQ
IIAGRQVCLL DQQEAEALRD RLQTQPWQVK SLEEKPTTRK PAPPFTTSTL QQESNRKLRL
SARETMRVAQ SLYERGFITY MRTDSVHLSQ QAIEAARSCV EQMYGKNYLS PQPRQFTTKS
KNAQEAHEAI RPAGNTFRLP QETGLSGAEF ALYDLIWKRT IASQMAEARQ TMLSVLLEVD
NAEFRASGKR IDFPGFFRAY VEGSDDPDAA LEDREILLPA LKVGDRPTCQ ELAAIGHETQ
PPARYTEASL VKMLENEGIG RPSTYASIIG TIVDRGYAQL VSNTLTPTFT AFAVTALLEQ
HFPDLVDTSF SARMEQSLDD ISNGEVDWLP YLSQFYRGDR GLEEQVKLRE SEIDPAAART
VALEGLPAKV RIGRFGAYLE AEADGEPIKA NLPKELTPAD LDVQRVETLL RQKTEGPDQL
GTHPETDEPI YLLTGAYGPY VQLGAATEEK PKPKRASLPK GMSLETISLE QAVGLLSLPR
TLGEHPETGR RIQAGLGRFG PYVVCDLGGG EKDYRSLKAD DDVLTIDLDR ALELLAQPKK
SRGRGKEPIR EVGLHPDDQA PIQIFEGPYG LYLKHGKVNA SLPEDEKPET ISLETAVAAL
AAKAGQAKAK GGRRSTGTPK SGETKARTTK TTKKTTTRRT TSR
