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Database: UniProt
Entry: C8WWD7_ALIAD
LinkDB: C8WWD7_ALIAD
Original site: C8WWD7_ALIAD 
ID   C8WWD7_ALIAD            Unreviewed;       696 AA.
AC   C8WWD7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 90.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952};
GN   OrderedLocusNames=Aaci_1381 {ECO:0000313|EMBL:ACV58408.1};
OS   Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 /
OS   DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 /
OS   NRRL B-14509 / 104-IA) (Bacillus acidocaldarius).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Alicyclobacillus.
OX   NCBI_TaxID=521098 {ECO:0000313|EMBL:ACV58408.1, ECO:0000313|Proteomes:UP000001917};
RN   [1] {ECO:0000313|Proteomes:UP000001917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC   15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC   {ECO:0000313|Proteomes:UP000001917};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Chertkov O., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete chromosome of Alicyclobacillus acidocaldarius subsp.
RT   acidocaldarius DSM 446.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACV58408.1, ECO:0000313|Proteomes:UP000001917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC
RC   15652 / NCIMB 11725 / NRRL B-14509 / 104-IA
RC   {ECO:0000313|Proteomes:UP000001917};
RX   PubMed=21304673; DOI=10.4056/sigs.591104;
RA   Mavromatis K., Sikorski J., Lapidus A., Glavina Del Rio T., Copeland A.,
RA   Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L.,
RA   Pitluck S., Ivanova N., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Meincke L.,
RA   Sims D., Chertkov O., Han C., Brettin T., Detter J.C., Wahrenburg C.,
RA   Rohde M., Pukall R., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Alicyclobacillus acidocaldarius type strain
RT   (104-IA).";
RL   Stand. Genomic Sci. 2:9-18(2010).
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:0000256|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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213, ECO:0000256|HAMAP-
CC         Rule:MF_00952};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}.
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DR   EMBL; CP001727; ACV58408.1; -; Genomic_DNA.
DR   RefSeq; WP_012810735.1; NC_013205.1.
DR   AlphaFoldDB; C8WWD7; -.
DR   STRING; 521098.Aaci_1381; -.
DR   KEGG; aac:Aaci_1381; -.
DR   eggNOG; COG0550; Bacteria.
DR   HOGENOM; CLU_002929_4_3_9; -.
DR   OMA; PECKYTR; -.
DR   Proteomes; UP000001917; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
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; 3.40.50.140; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 2.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 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; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 3.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 2.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00952};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001917};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00952}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          3..114
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          163..168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   ACT_SITE        298
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            33
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            139
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            140
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            143
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            148
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            155
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            300
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            491
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   696 AA;  78936 MW;  A38176B332177AAC CRC64;
     MSDYLVIVES PAKAKTIGKY LGSKYTVKAS MGHVRDLPKS QLGVDVEHGF EPKYITIRGK
     GDVIKALREA SKKAKKVYLA ADPDREGEAI AWHLQHLLDL NPDDDCRVVF HEITKDAVKQ
     AFQHPRKINL DLVNAQQTRR ILDRLVGYKL SPLLWRKVKK GLSAGRVQSV ALRLIVDREN
     EIRTFQPEEY WTVDAHGQVH GKKLVARFYG YGEEKTPLPN EAAVRELLSR VEGHSLVVRR
     VKKSERKRNP AAPFTTSSLQ QEAARKLGFR AYKTMQIAQQ LYEGLDVPGE GTVGLITYMR
     TDSTRIAQSA QEEARAYIRQ SFGEDYVPDR PRQYAKNEDA QDAHEAIRPT SVMRHPDRLK
     DHLSRDQYRL YKLIWERFVA SQMESAVLDT TSVDLEANGA WFRATGSVVR FPGFMALYTE
     GRDDDADEEE GKLLPPLQEG DVVQVKTWKP EQHFTQPPPR YTESTLVKAM EELGIGRPST
     YAPTIDILLK RGYVTLDQKR FVPTELGEIV VNILKEHFPQ LIDVSFTADM ESRLDKVEEG
     NANWIELLDQ FYHDFEKDLK KAESALGHVE LKDEVSDVRC EKCGRLMVYK TGRYGKFLAC
     PGFPECRNTK PILKEIPVSC PKCGKPLVER KGKSRKVFYG CSGYPECDYV LWQRPTGQTC
     PVCGHPMIEK GGKGKTVVVC SNEKAHPMVA TEAQAK
//
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