ID A0A2Z4LQC4_9FLAO Unreviewed; 829 AA.
AC A0A2Z4LQC4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=HME9304_00971 {ECO:0000313|EMBL:AWX43972.1};
OS Allomuricauda aurantiaca.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1383885 {ECO:0000313|EMBL:AWX43972.1, ECO:0000313|Proteomes:UP000248536};
RN [1] {ECO:0000313|EMBL:AWX43972.1, ECO:0000313|Proteomes:UP000248536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HME9304 {ECO:0000313|EMBL:AWX43972.1,
RC ECO:0000313|Proteomes:UP000248536};
RA Kang H., Kim H., Joh K.;
RT "Spongiibacterium sp. HME9304 Genome sequencing and assembly.";
RL Submitted (JUN-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}.
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DR EMBL; CP030104; AWX43972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4LQC4; -.
DR KEGG; spon:HME9304_00971; -.
DR OrthoDB; 9804262at2; -.
DR Proteomes; UP000248536; Chromosome.
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; 2.
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; 2.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF13368; Toprim_C_rpt; 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 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:UP000248536};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00952}.
FT DOMAIN 3..113
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 284
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 286
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT SITE 475
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ SEQUENCE 829 AA; 93691 MW; EB5DF8A562E9A135 CRC64;
MPKNLVIVES PAKAKTIERF LGKDYQVESS FGHIADLPSK ELGVDVENNF KPKYTVDKDK
RALVKKLKDL AKKADTIWLA SDEDREGEAI SWHLAEELGL DKSKTKRIVF NSITKSAIQN
AIDNPREINY NLVNAQQARR VLDRLVGYEL SPVLWKKIKP GLSAGRVQSV SVRLIVERER
DIEAFTPEAS FKIQAEFSTS NGNTFSAKLN KTFPNKEAAH TFLKQNIGAN FSVASLDKKP
AKKSPAAPFT TSTLQQEASR KLYFSVGRTM QVAQRLYEAG LITYMRTDSV NLSKEALTAA
KDAIVHNYGE SYSKVRNYTG KSKGAQEAHE AIRPTDMKLN APSLERDQSK LYELIWKRTL
ASQMSDAELE RTNVKIKASS HNEEFSANGE VVKFDGFLKV YLEGTDEEDK TEEQEGMLPA
MKIGETLRNN FITATERFSR PPYRYTEASL VKKLEELGIG RPSTYAPTIS TIQNRGYVEK
GTVEGTERNY TQLLLEDDKL EEKKLSEMVG SDKGKLVPTD IGMIVNDFLV DHFTTILDYN
FTAKVEEDFD EIAAGEEDWQ KMMKEFYEDF HPNVLEVEEN AERASGERVL GTDPKSGRQV
AARLGRFGPM VQIGTVDEEE KPLFASLLPD QSITTITFDE AMKLFELPKK LGVYEGEEVE
TNVGRFGPYV RFGKKFISLD KGESAFDVDM DRAIELIKAK QKADAPIAHY EDKEVTKGVG
RFGPFIKWDG MFINVNKKYN FDNLSKSDIV ELIEAKKIKE AEKLIQEWPE EKIRIEKARW
GRHNIIKGKI KVELSKDVDA TKISLKEAQA LIEKKSPKKK TKAKPKAKK
//
