ID N6X382_9ACTO Unreviewed; 906 AA.
AC N6X382;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 ECO:0000313|EMBL:ENO18151.1};
GN ORFNames=HMPREF9004_1095 {ECO:0000313|EMBL:ENO18151.1};
OS Schaalia cardiffensis F0333.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Schaalia.
OX NCBI_TaxID=888050 {ECO:0000313|EMBL:ENO18151.1, ECO:0000313|Proteomes:UP000013015};
RN [1] {ECO:0000313|EMBL:ENO18151.1, ECO:0000313|Proteomes:UP000013015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0333 {ECO:0000313|EMBL:ENO18151.1,
RC ECO:0000313|Proteomes:UP000013015};
RA Aqrawi P., Ayvaz T., Bess C., Blankenburg K., Coyle M., Deng J., Forbes L.,
RA Fowler G., Francisco L., Fu Q., Gibbs R., Gross S., Gubbala S., Hale W.,
RA Hemphill L., Highlander S., Hirani K., Jackson L., Jakkamsetti A.,
RA Javaid M., Jayaseelan J.C., Jiang H., Joshi V., Korchina V., Kovar C.,
RA Lara F., Lee S., Liu Y., Mata R., Mathew T., Munidasa M., Muzny D.,
RA Nazareth L., Ngo R., Nguyen L., Nguyen N., Okwuonu G., Ongeri F.,
RA Palculict T., Patil S., Petrosino J., Pham C., Pham P., Pu L.-L., Qin X.,
RA Qu J., Reid J., Ross M., Ruth R., Saada N., San Lucas F., Santibanez J.,
RA Shang Y., Simmons D., Song X.-Z., Tang L.-Y., Thornton R., Warren J.,
RA Weissenberger G., Wilczek-Boney K., Worley K., Youmans B., Zhang J.,
RA Zhang L., Zhao Z., Zhou C., Zhu D., Zhu Y.;
RT "Reference genome for the Human Microbiome Project.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENO18151.1}.
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DR EMBL; AQHZ01000017; ENO18151.1; -; Genomic_DNA.
DR RefSeq; WP_005963182.1; NZ_KB822674.1.
DR AlphaFoldDB; N6X382; -.
DR STRING; 888050.HMPREF9004_1095; -.
DR PATRIC; fig|888050.3.peg.1039; -.
DR eggNOG; COG0550; Bacteria.
DR HOGENOM; CLU_002929_2_0_11; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000013015; Unassembled WGS sequence.
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; 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; IPR005733; TopoI_bac-type.
DR InterPro; IPR028612; Topoisom_1_IA.
DR InterPro; IPR025589; Toprim_C_rpt.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034149; TOPRIM_TopoI.
DR NCBIfam; TIGR01051; topA_bact; 1.
DR PANTHER; PTHR42785:SF1; DNA TOPOISOMERASE; 1.
DR PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 4.
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 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:UP000013015};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 4..127
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 176..181
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 449..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 878..906
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 324
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 34
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 152
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 153
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 156
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 161
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 168
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 326
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 532
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 906 AA; 99077 MW; 27A083707418DBDF CRC64;
MGASKLVIVE SPAKAATIEG YLGPDYHVTA SIGHIRDLPQ PKDLPTEMKK GPYGRFAVDV
EHGFTPYYAV NPDKKKKVAE LRKALKESDE LFLATDEDRE GEAIAWHLLQ VLKPKVPVKR
MVFHEITKEA ITRALENTRE LDTALVDAQE TRRVLDRLYG YEVSPLLWRK IRPSLSAGRV
QSVATRLVVD RERDRMAHVS ASYCSISTRI EAGAESFDAR VTHVDGRAVA GGSDFSEKGV
LKEKAEKAGV LHLDEAFAAS IAQALEASPS SIIESVTQKP YRRRPAAPFT TSTLQQEASR
KLHWNASSTM RTAQSLYESG YITYMRTDST ALSSQAIQAA RAQAAELYGA DSVPEKPRFY
GNVSKGAQEA HEAIRPAGDH FRTPAEVSSL LSKQQLALYD LIWKRTLASQ MTDALGFTAT
IRVLTGISVE GERHDVISSA SGTVITHPGF RQAYQEGRDK GRYDQEKDSG SEKVLPNVSE
GEDADVVEAK PEGHETQPPG RYTEATLVKT MEERGIGRPS TYAATIQTIG DRGYIVHRGQ
YLVPTWLAFS VTRLLEENLS NLVDYDFTAS METDLDRIAA GEESGEEFLS LFYLGANGEG
DADGLKFQVE SLGDDIDARA VNSQEVGEGV VVRVGRYGPY LEKADGTRAN LPEDVAPDEV
DAKKIEELFA LAADDGRELG IDPATGHTLI AKNGRFGPYI TEILPEEEEP TTNGKGKKKA
AAPKPRTASL FKSMDLRTVT LEQALELLSL PRELGVDPAS GEVITAQNGR YGPYLKKGSD
SRTLSSEEQL LSITLDEALA IYAQPKTRGR GAAKPPLREF DADPVSGKKV VVKDGRFGPY
VTDGETNVTV PRAESVEDLT QERAFELLAD KRTKGPAPKK ATRTTRKTTA KKTASKKTST
KKASTK
//
