ID TOP1_HAEIN Reviewed; 868 AA.
AC P43012;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 01-MAY-2013, entry version 105.
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=HI_1365;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=8635745; DOI=10.1016/0378-1119(95)00777-6;
RA Chandler M.S., Smith R.A.;
RT "Characterization of the Haemophilus influenzae topA locus: DNA
RT topoisomerase I is required for genetic competence.";
RL Gene 169:25-31(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
RA Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
RA Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
RA Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
RA Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
RA Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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 (By similarity).
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC -!- SIMILARITY: Contains 1 Toprim domain.
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DR EMBL; U20964; AAC43727.1; -; Genomic_DNA.
DR EMBL; L42023; AAC23012.1; -; Genomic_DNA.
DR PIR; G64119; G64119.
DR RefSeq; NP_439516.1; NC_000907.1.
DR ProteinModelPortal; P43012; -.
DR SMR; P43012; 3-598, 748-868.
DR STRING; 71421.HI1365; -.
DR PRIDE; P43012; -.
DR EnsemblBacteria; AAC23012; AAC23012; HI_1365.
DR GeneID; 950025; -.
DR KEGG; hin:HI1365; -.
DR PATRIC; 20191417; VBIHaeInf48452_1419.
DR eggNOG; COG0551; -.
DR KO; K03168; -.
DR OMA; EFWDIHA; -.
DR ProtClustDB; PRK07561; -.
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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:InterPro.
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; IPR013498; Topo_IA_Znf.
DR InterPro; IPR005733; TopoI_bac-type.
DR InterPro; IPR013263; TopoI_Znr_bac.
DR InterPro; IPR006171; Toprim_domain.
DR PANTHER; PTHR11390; PTHR11390; 1.
DR Pfam; PF08272; Topo_Zn_Ribbon; 2.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF01396; zf-C4_Topoisom; 2.
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; Reference proteome; Repeat;
KW Topoisomerase; Zinc; Zinc-finger.
FT CHAIN 1 868 DNA topoisomerase 1.
FT /FTId=PRO_0000145149.
FT DOMAIN 3 148 Toprim.
FT ZN_FING 605 636 C4-type 1.
FT ZN_FING 667 694 C4-type 2.
FT ZN_FING 716 739 C4-type 3.
FT REGION 198 203 Interaction with DNA (By similarity).
FT ACT_SITE 325 325 O-(5'-phospho-DNA)-tyrosine intermediate
FT (By similarity).
FT METAL 9 9 Magnesium 1; catalytic (By similarity).
FT METAL 117 117 Magnesium 1; catalytic (By similarity).
FT METAL 117 117 Magnesium 2 (By similarity).
FT METAL 119 119 Magnesium 2 (By similarity).
FT SITE 33 33 Interaction with DNA (By similarity).
FT SITE 174 174 Interaction with DNA (By similarity).
FT SITE 175 175 Interaction with DNA (By similarity).
FT SITE 178 178 Interaction with DNA (By similarity).
FT SITE 190 190 Interaction with DNA (By similarity).
FT SITE 327 327 Interaction with DNA (By similarity).
FT SITE 513 513 Interaction with DNA (By similarity).
FT CONFLICT 343 343 T -> S (in Ref. 2; AAC23012).
SQ SEQUENCE 868 AA; 98144 MW; AAD604BDEBC75D20 CRC64;
MSKSLVIVES PAKAKTINKY LGSQYVVKSS VGHIRDLPTV GSSTGEKAKP ISTKGMDAEE
KAKIKAEKER NALVKRMGID PYHDWKANYQ ILPGKEKVVS ELKSLAKKAD HIYLATDLDR
EGEAIAWHLR EVIGGNDDRF SRVVFNEITK NAIKQAFEKP EQLNMDRVNA QQTRRFLDRV
VGFMVSPLLW KKVARGLSAG RVQSVAVKLL VEREREIKAF QPEEYWEVAV LTNNQNKQAI
RLDVTDYKGK KFDPKNQKEA QSAVDFLNVS DYVVTDLETK PTSSRPRAPF ITSTLQQTAS
TRLGFGVKKT MMLAQRLYEA GYITYMRTDS TNLSQDALNM ARTYIENHFG AQYLPEKPNF
YSSKENAQEA HEAIRPSDIR ALPESLEGME KDAVRLYDLI WCQFLACQMP PAQYDSSTLT
VTAGDYTLKA KGRILRFDGW TKVLPQIGKN PEDQELPSVT VSEKLALKEV QPTQHFTKPP
ARFTEAALVK ELEKRGIGRP STYAAIISTI QERGYVRTEN RRFYAEKMGE IVTDRLNESF
GELMNYDFTA NMEDTLDKIA SGSVNWKTEL NQFFKDFSSQ LSKAELDELE GGMRPNSLVE
TDIKCPTCGR NMAIRTASTG VFLGCTGYAL PPKERCKTTI NLIPEAELLN VLDESSETKA
LMDRKRCTKC GTAMDSYVID AHRKIHICGN NPNCDGYLIE EGSFKIKGYD GPVVECDKCG
ADMHLKLGRF GKYMGCTNCD NTRKILKNGE VAPPKEEPVH FPELKCEKSD AYFVLRDGAS
GVFMSAHNFP KSRETRPVKI AELVQYRERL PEKLAYLADA PQKDPEENEA IVRFSRKEKK
QYVTSEKEGK ATKWIVDFTN GKWVERKK
//
