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Database: UniProt
Entry: P43012
LinkDB: P43012
Original site: P43012 
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   03-SEP-2014, entry version 115.
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; VVECDKC; -.
DR   OrthoDB; EOG6S7XQ9; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   Gene3D; 1.10.460.10; -; 2.
DR   Gene3D; 2.70.20.10; -; 2.
DR   Gene3D; 3.40.50.140; -; 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; 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; IPR028612; Topoisom_1_IA.
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; 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   Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW   Reference proteome; Repeat; 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
//
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