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 01-MAY-2013, entry version 92.
DE RecName: Full=DNA topoisomerase 1;
DE EC=5.99.1.2;
DE AltName: Full=DNA topoisomerase I;
DE AltName: Full=Omega-protein;
DE AltName: Full=Relaxing enzyme;
DE AltName: Full=Swivelase;
DE AltName: Full=Untwisting enzyme;
GN Name=topA; OrderedLocusNames=Synpcc7942_1416;
OS Synechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2).
OC Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC 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
RT genes involved in the ability to grow under low CO2 concentration and
RT in chlorophyll biosynthesis.";
RL Plant Physiol. 108:1461-1469(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942;
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
RT 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA,
CC which is introduced during the DNA replication and transcription,
CC by transiently cleaving and rejoining one strand of the DNA
CC duplex. Introduces a single-strand break via transesterification
CC at a target site in duplex DNA. The scissile phosphodiester is
CC attacked by the catalytic tyrosine of the enzyme, resulting in the
CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the
CC expulsion of a 3'-OH DNA strand. The free DNA strand then
CC undergoes passage around the unbroken strand, thus removing DNA
CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks
CC the covalent intermediate to expel the active-site tyrosine and
CC restore the DNA phosphodiester backbone (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC DNA, followed by passage and rejoining.
CC -!- COFACTOR: Magnesium. Binds two Mg(2+) per subunit (By similarity).
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC -!- SIMILARITY: Contains 1 Toprim domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA51086.1; Type=Frameshift; Positions=Several;
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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; YP_400433.1; NC_007604.1.
DR ProteinModelPortal; P34185; -.
DR STRING; 1140.Synpcc7942_1416; -.
DR EnsemblBacteria; ABB57446; ABB57446; Synpcc7942_1416.
DR GeneID; 3774129; -.
DR KEGG; syf:Synpcc7942_1416; -.
DR PATRIC; 23788179; VBISynElo51371_1616.
DR eggNOG; COG1754; -.
DR HOGENOM; HOG000004020; -.
DR KO; K03168; -.
DR ProtClustDB; PRK07561; -.
DR BioCyc; SELO1140:GJWQ-1440-MONOMER; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 1.10.460.10; -; 2.
DR Gene3D; 2.70.20.10; -; 2.
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; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR003602; Topo_IA_DNA-bd.
DR InterPro; IPR005733; TopoI_bac-type.
DR InterPro; IPR006171; Toprim_domain.
DR PANTHER; PTHR11390; PTHR11390; 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; Topo_IA_core; 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 ATP-binding; Complete proteome; DNA-binding; Isomerase; Magnesium;
KW Metal-binding; Nucleotide-binding; Topoisomerase.
FT CHAIN 1 883 DNA topoisomerase 1.
FT /FTId=PRO_0000145167.
FT DOMAIN 2 126 Toprim.
FT REGION 175 180 Interaction with DNA (By similarity).
FT ACT_SITE 320 320 O-(5'-phospho-DNA)-tyrosine intermediate
FT (By similarity).
FT METAL 8 8 Magnesium 1; catalytic (By similarity).
FT METAL 95 95 Magnesium 1; catalytic (By similarity).
FT METAL 95 95 Magnesium 2 (By similarity).
FT METAL 97 97 Magnesium 2 (By similarity).
FT SITE 32 32 Interaction with DNA (By similarity).
FT SITE 151 151 Interaction with DNA (By similarity).
FT SITE 152 152 Interaction with DNA (By similarity).
FT SITE 155 155 Interaction with DNA (By similarity).
FT SITE 160 160 Interaction with DNA (By similarity).
FT SITE 167 167 Interaction with DNA (By similarity).
FT SITE 322 322 Interaction with DNA (By similarity).
FT SITE 515 515 Interaction with DNA (By similarity).
FT CONFLICT 101 102 ES -> KV (in Ref. 1; CAA51086).
FT CONFLICT 392 392 L -> V (in Ref. 1; CAA51086).
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
//
