ID A9IMQ7_BORPD Unreviewed; 338 AA.
AC A9IMQ7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
GN Name=topI {ECO:0000313|EMBL:CAP42738.1};
GN OrderedLocusNames=Bpet2395 {ECO:0000313|EMBL:CAP42738.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42738.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP42738.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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};
CC -!- SIMILARITY: Belongs to the type IB topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00006645}.
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DR EMBL; AM902716; CAP42738.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IMQ7; -.
DR STRING; 94624.Bpet2395; -.
DR KEGG; bpt:Bpet2395; -.
DR eggNOG; COG3569; Bacteria.
DR Proteomes; UP000001225; 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:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 1.10.132.120; -; 1.
DR Gene3D; 3.30.66.10; DNA topoisomerase I domain; 1.
DR InterPro; IPR011010; DNA_brk_join_enz.
DR InterPro; IPR035447; DNA_topo_I_N_sf.
DR InterPro; IPR049331; Top1B_N_bact.
DR InterPro; IPR001631; TopoI.
DR InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR InterPro; IPR013500; TopoI_cat_euk.
DR Pfam; PF21338; Top1B_N_bact; 1.
DR Pfam; PF01028; Topoisom_I; 1.
DR PRINTS; PR00416; EUTPISMRASEI.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 1.
DR SUPFAM; SSF55869; DNA topoisomerase I domain; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 26..74
FT /note="DNA topoisomerase IB N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21338"
FT DOMAIN 86..295
FT /note="DNA topoisomerase I catalytic core eukaryotic-type"
FT /evidence="ECO:0000259|Pfam:PF01028"
SQ SEQUENCE 338 AA; 38038 MW; 10D25AD29A17B8A6 CRC64;
MARQAGLVYV DDSRPGYTRE RARSGGFRYL DTRGRVISDA RVIARIDALA IPPAYTDVWI
CPLPNGHLQA TGRDARGRKQ YRYHADWRAE RDAAKYGQLL EFAASLPRIR RRVARDMRRP
ALTQDKMLAV LVRLLEITLI RIGTREYARA NQSYGLTTLK RRHTAVAGDR LRLRFTGKSG
VAHDVTVTDA RIARTVKRCM DLPGQQLFHY RAEDGEIRPV DSDMVNAYLK AASGSGFTAK
HYRTWAGSVM AFKLLQGQPV DNDAQATRTL AEVVRQVAKR LGNTPAVCRN CYIHPTILDA
YRLGALPACT TPAAAPRGLA ADERRLWHFL RSWQAPRT
//
