TOP1_ALKPO
ID TOP1_ALKPO Reviewed; 707 AA.
AC P34184; D3G1M5; D3G1M6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA topoisomerase 1;
DE EC=5.6.2.1 {ECO:0000255|PROSITE-ProRule:PRU10131};
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=BpOF4_21279/BpOF4_21284;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OG Plasmid pBpOF4-01.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4; PLASMID=pBpOF4-01;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-706.
RX PubMed=1329032; DOI=10.1093/nar/20.18.4928;
RA Ivey D.M., Cheng J., Krulwich T.A.;
RT "A 1.6 kb region of Bacillus firmus OF4 DNA encodes a homolog of
RT Escherichia coli and yeast DNA topoisomerases and may contain a
RT translational readthrough of UGA.";
RL Nucleic Acids Res. 20:4928-4928(1992).
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 (By similarity). {ECO:0000250}.
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|PROSITE-
CC ProRule:PRU10131};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. {ECO:0000305}.
CC -!- CAUTION: The sequence displayed is the result of a readthrough of the
CC terminator UGA between codons for Tyr-288 and Leu-290. However,
CC translational readthrough of UGA in this protein has not been proven.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADC52251.1; Type=Miscellaneous discrepancy; Note=Probable readthrough of the stop codon.; Evidence={ECO:0000305};
CC Sequence=ADC52252.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA78484.1; Type=Miscellaneous discrepancy; Note=Probable readthrough of the stop codon.; Evidence={ECO:0000305};
CC Sequence=CAA78485.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA78485.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CP001879; ADC52251.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP001879; ADC52252.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z14112; CAA78484.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z14112; CAA78485.1; ALT_SEQ; Genomic_DNA.
DR PIR; S23866; S23866.
DR STRING; 398511.BpOF4_21284; -.
DR EnsemblBacteria; ADC52251; ADC52251; BpOF4_21279.
DR EnsemblBacteria; ADC52252; ADC52252; BpOF4_21284.
DR KEGG; bpf:BpOF4_21279; -.
DR KEGG; bpf:BpOF4_21284; -.
DR eggNOG; COG0550; Bacteria.
DR HOGENOM; CLU_002929_5_0_9; -.
DR Proteomes; UP000001544; Plasmid pBpOF4-01.
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; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR Gene3D; 1.10.290.10; -; 1.
DR Gene3D; 1.10.460.10; -; 1.
DR Gene3D; 2.70.20.10; -; 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; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR PANTHER; PTHR11390; PTHR11390; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13342; Toprim_Crpt; 1.
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 PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA-binding; Isomerase; Plasmid; Reference proteome;
KW RNA suppression of termination; Topoisomerase.
FT CHAIN 1..706
FT /note="DNA topoisomerase 1"
FT /id="PRO_0000145140"
FT DOMAIN 1..140
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT REGION 199..204
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 323
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT SITE 48
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 167
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 171
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 325
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT SITE 529
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT CONFLICT 126
FT /note="Q -> H (in Ref. 2; CAA78484)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="T -> F (in Ref. 2; CAA78484)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="I -> L (in Ref. 2; CAA78484)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="K -> T (in Ref. 2; CAA78484)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> D (in Ref. 2; CAA78484)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="F -> S (in Ref. 2; CAA78485)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="W -> R (in Ref. 2; CAA78485)"
FT /evidence="ECO:0000305"
FT CONFLICT 523..524
FT /note="IT -> TH (in Ref. 2; CAA78485)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="V -> A (in Ref. 2; CAA78485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 707 AA; 80296 MW; 1E07919E5AD9AA00 CRC64;
MYAILAEKPS AAKAYAQALN GKRQGRIYVA PPSSLLPEGA LICAAVGHIL EFLEPGELNE
KYKSYSLDSL PIIIDLFQYK VVSDKKEVLQ RIKDTIFDKR VKTIILATDA AAEGEYIGRN
ILYRLQCKKT IKRLWTSSMT ATSIQKAFSQ LKADAETLPL YYQAKARAES DYMIGLTLSR
AYGILLKEQG IVPHNTTISL GRVQTPLLAE IVKRERLIEQ FTAENFWTVK ATFNNQGNVY
EGEWFHEKEN RIFKEEQAEQ LCELVRNQSS TIMEMKEEMR TYQPPLLYXL STLQMDAGNA
FGFKPAETLK YAQSLYDKGY LSYPRTQDER ITESDARELE NNIQFLSGHD TFGALFPLPV
STLMNNKRYI GEVTDHHALL ITDKIPKDKD LSEDEKSIYH LVVKRILAAH YPDVAMSHKE
IITKVMDRFT FRSKGKELLS KGWHHIIPPT NENDIMLPTL LKGSEGVVTD TLTTKSKTKP
PNRYTSSSLI GFMKNAAQAI EDEDRKSISN LPLGTEATRA GLITLLESRK YIEWKKNKVY
PTLLGITVVD SIKRGSVIKS PILTAKWDVK LNEIGASLYN HKDFIAHSKK LSSVLFEEVK
TYSSTWNQNG VERIKSESIG ACLLCGSNVV LRKGKHGEFY GCSNYKDSGC TFNLPFKVLN
KKLSKKQLME LLKNEKTDII KGFKWKDKTF NAPLVWNRED QKVQFGK
