ID A0Z9F8_9GAMM Unreviewed; 919 AA.
AC A0Z9F8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=MGP2080_12317 {ECO:0000313|EMBL:EAW39402.1};
OS marine gamma proteobacterium HTCC2080.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=247639 {ECO:0000313|EMBL:EAW39402.1, ECO:0000313|Proteomes:UP000004719};
RN [1] {ECO:0000313|EMBL:EAW39402.1, ECO:0000313|Proteomes:UP000004719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2080 {ECO:0000313|EMBL:EAW39402.1,
RC ECO:0000313|Proteomes:UP000004719};
RX PubMed=20472793; DOI=10.1128/jb.00511-10;
RA Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT OM60/NOR5 clade of the Gammaproteobacteria.";
RL J. Bacteriol. 192:3842-3843(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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:EAW39402.1}.
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DR EMBL; AAVV01000021; EAW39402.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Z9F8; -.
DR eggNOG; COG0550; Bacteria.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000004719; 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:UP000004719};
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..153
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 203..208
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT REGION 874..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..900
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 330
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 179
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 183
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 195
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 332
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 518
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 919 AA; 102218 MW; C85BA8752E5F48CF CRC64;
MPKSLVIVES PAKAKTINKY LGNDFIVKSS VGHIRDLPTS GSATSSDPKE RAAQAALTRK
MAPEAKKRYQ DKKKREQLVR RMGIDPDHDW NARYEVLPGK EKVVSELRRL AEKSDAIYLA
TDLDREGEAI AWHLREAIGG DESRYQRVVF NEITKKAIQE AFQKPTELDT NRVNAQQARR
FLDRVVGFEV SPLLWAKVAR GLSAGRVQSV AVRLVVERER EIRAFVPDEY WEVHANLLPE
GFEAVRFEVK YRAGAKFAPK TETEAMTAVA ALEAATFEVS NLEARKTSSK PGAPFITSTL
QQSASTRLGF SVKKTMTLAQ RLYEAGYITY MRTDSTNLSN DAVAACRQYI GKNYSGDYLP
EAPLRYSSKE GAQEAHEAIR PSDVRVTQND LQGMERDAER LYELIWRQFV ACQMTPARYR
STTVTVAAAD YGLTARGRVV EFDGFTRVQA PMSRKGDDAE LPALTVGETL KLQQVDPKQH
FTKPPARYGE ASLVREMEKR SIGRPSTYAA IISTIQDRGY VRLENRRLYA EKMGDIVTQR
LQASFADLLD YGFTASMEAN LDDVADGRLN WKDLLNDFYG DFRGKLDQAG SPDPGGMQLN
DPTPTGIPCG TCDRPMQIRT ASTGVFLGCS GYSLPPKERC KSTLNLTSGD EAISADADDE
AESRLLLQKR RCGLCNTAMD SYLIDEERKL HVCGNNPDCP GYEVESGKFR IKGYDGPTIE
CDKCAADMQL KTGRFGKYFG CTNAECKNTR KLLRSGEAAP PKMDPVPMPE LDCIKVEDHY
ILRDGASGLF LAASKFPKNR ETRPPFVDEL LPHQGEIDPK YHFLFDAPLT DDAGNRSQIR
YSRKTKEQYV MTDVDGKATG WKAFFDNGAW QVSGTAKAPK KKAAPKKKAK AKKKAVAKKT
PATKRASLAG DGSKPLSEG
//
