ID F3LFW1_9GAMM Unreviewed; 935 AA.
AC F3LFW1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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=IMCC1989_194 {ECO:0000313|EMBL:EGG94216.1};
OS gamma proteobacterium IMCC1989.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales.
OX NCBI_TaxID=937772 {ECO:0000313|EMBL:EGG94216.1, ECO:0000313|Proteomes:UP000010300};
RN [1] {ECO:0000313|EMBL:EGG94216.1, ECO:0000313|Proteomes:UP000010300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1989 {ECO:0000313|EMBL:EGG94216.1,
RC ECO:0000313|Proteomes:UP000010300};
RX PubMed=21602334; DOI=10.1128/JB.05202-11;
RA Jang Y., Oh H.M., Kim H., Kang I., Cho J.C.;
RT "Genome sequence of strain IMCC1989, a novel member of the marine
RT gammaproteobacteria.";
RL J. Bacteriol. 193:3672-3673(2011).
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:EGG94216.1}.
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DR EMBL; AEVK01000105; EGG94216.1; -; Genomic_DNA.
DR AlphaFoldDB; F3LFW1; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000010300; 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; 2.20.25.10; -; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 3.
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; IPR049330; TOP1_Znf.
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; IPR013263; TopoI_Znr_bac.
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; PF21372; TOP1_ZnF; 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; Prokaryotic type I DNA topoisomerase; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 3.
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:UP000010300};
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..154
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 204..209
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 892..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..935
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
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 180
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 181
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 184
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 189
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 196
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 333
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 519
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 935 AA; 104077 MW; 5F1A944972BDCD31 CRC64;
MGKSLVIVES PAKAKTINKY LGNDFIVKSS IGHIRDLPTS GSSKTPVDAK ARAKQAALTR
KMSPEDKVIH KAKKSREQLI KRMGIDPDNN WAAHYEILPG KEKVVDELKK LAASADTIYL
ATDLDREGEA IAWHLQQAIG GDESRYRRVV FNEITKTAIQ KAFETPGYLD QHRVDAQQAR
RFLDRVVGYM VSPLLWEKVA RGLSAGRVQS VAVRLVVERE REIRAFIPEE YWDVFASLLT
ADKSTVRCEV KKQKGNAFRP NNSDDCMASV AELENATFTV VKRDDKPTSS KPSSPFITST
LQQTASTRLG FGVKKTMMMA QRLYEAGYIT YMRTDSTNLS QEAVASCRDY ILENYGKRYL
PEAPINYSSK EGAQEAHEAI RPSNVSVSPT QLSGMERDAE RLYTLIWQQF VACQMTRAEF
TSTSVVIQAG DFELRTRGRV IRFDGFMRVQ PPAGKKEDDV LLPDVAVGDV LSLKALEPKQ
HFTKPTARYT EASLVKELEK QGIGRPSTYA SIISTIQDRG YAHVESRRFF ADKMGDIVTD
RLVENFDDLL DYGFTAKMEE SLDSVADGQI EWRDLLNQFY TGFVDKLKQA QQAENGMRLN
SPTETDISCS TCSRPMQIRT ASTGVFLGCS GYALPPKERC KTTMNLVSGD EAVSVDTNVA
SGSGASESDE TAAEEAEVRQ LRNKRRCSIC NTAMDSYLLD ETRKLHICGN NPDCSGYEVE
TGTFKIKGYE GPVLDCDKCG SEMQLKTGRF GKYFGCTNEE CKNTRKLLRN GEAAPPKMDP
VPMPELECVK VDDTYILRDG ASGLFLAASQ FPKNRETRAP LVAEIIPHKD EIDNKYNFLF
SAPTEDDDGN PTLIRFSRKT KEQYVQSEVD GKATGWKAFY EGGKWVVSAA PVKRKAAPKK
KAAPKKKAAP KKKATAKKKA APKKKAVAKK SPAKE
//
