ID A0A174AIQ5_9FIRM Unreviewed; 694 AA.
AC A0A174AIQ5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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 ORFNames=C4N23_07485 {ECO:0000313|EMBL:RAW61823.1}, CGS58_00375
GN {ECO:0000313|EMBL:PDX82663.1};
OS Faecalibacterium prausnitzii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Faecalibacterium.
OX NCBI_TaxID=853 {ECO:0000313|EMBL:RAW61823.1, ECO:0000313|Proteomes:UP000250429};
RN [1] {ECO:0000313|EMBL:PDX82663.1, ECO:0000313|Proteomes:UP000220005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I 4575 {ECO:0000313|EMBL:PDX82663.1,
RC ECO:0000313|Proteomes:UP000220005};
RX PubMed=28970823; DOI=10.3389/fmicb.2017.01790;
RA Benevides L., Burman S., Martin R., Robert V., Thomas M., Miquel S.,
RA Chain F., Sokol H., Bermudez-Humaran L.G., Morrison M., Langella P.,
RA Azevedo V.A., Chatel J.M., Soares S.;
RT "New Insights into the Diversity of the Genus Faecalibacterium.";
RL Front. Microbiol. 8:1790-1790(2017).
RN [2] {ECO:0000313|EMBL:PDX82663.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNCM I 4575 {ECO:0000313|EMBL:PDX82663.1};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RAW61823.1, ECO:0000313|Proteomes:UP000250429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APC922/41-1 {ECO:0000313|EMBL:RAW61823.1,
RC ECO:0000313|Proteomes:UP000250429};
RA Fitzgerald B.C., Shkoporov A.N., Ross P.R., Hill C.;
RT "Complete genome sequencing of Faecalibacterium prausnitzii strains
RT isolated from the human gut.";
RL Submitted (FEB-2018) 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:RAW61823.1}.
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DR EMBL; NMTY01000003; PDX82663.1; -; Genomic_DNA.
DR EMBL; PRLC01000009; RAW61823.1; -; Genomic_DNA.
DR RefSeq; WP_055190590.1; NZ_NMTY01000003.1.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000220005; Unassembled WGS sequence.
DR Proteomes; UP000250429; Unassembled WGS sequence.
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: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; 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; 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 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 2..112
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 162..167
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 32
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 138
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 142
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 147
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 154
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 694 AA; 77419 MW; 6D5CEDE351E8FD0A CRC64;
MSKLVIVESP AKAKTIGKYL GKDYEVTASM GHIRDLPASQ LGIDVEHDYT PQYISIKGKE
KLIKELKSKA KHSDGVLLAT DPDREGEAIS WHLANILGLD PHEPNRVTFD EITKKGVQEG
MAHPRAIDED LFNAQQARRV LDRLVGYKLS PFLWRKVRRG LSAGRVQSVA VRLIDDREKE
IESFKPEEYW NVDATLGVGH KSFTARLASD DKGKKLLPRT EAEARAIEQG LEGAEYTVGE
LKKGKRAKQP TPAFITSTLQ QEASRRLGFT ATRTMRAAQT LYEGVDIAGH GTMGLITYMR
TDSLRISDEA VAAAKEYIAG AYGEQYICPY KRTWKTKSAT AAQDAHEAIR PSVPSLTPDE
VDKSISGDTA KLYRMIWSRF MASQMADCQQ DTVSVTVYAG GYRFKASGYT VTFDGFTALY
EEATDEKEKK ETSLPPLEQG QVLKLRELKS EQKFTQPPAR YTEATLIKAL EENGIGRPST
YAPIITTIID RGYVERDQKK LKPTLLGRAV DGLMLEQFPH IVDVDFSAEM EKNLDKVESG
KADWHKTVDD FYQGFAASLE QAEKNMEGKK VKVPDEPSSE VCDLCGRPMV IKVGKYGKFL
ACSGFPECRG TKRLVKDTGG ICPKCGKGRM LERKSAKGRI YYGCERYPDC DFMTWDTPVP
IKCEKCGSTL FRKGSKLYCA KEGCGFEMPV PKKD
//
