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Database: UniProt
Entry: Q122E9_POLSJ
LinkDB: Q122E9_POLSJ
Original site: Q122E9_POLSJ 
ID   Q122E9_POLSJ            Unreviewed;       992 AA.
AC   Q122E9;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE   AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE   AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE   AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE   AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN   OrderedLocusNames=Bpro_4713 {ECO:0000313|EMBL:ABE46593.1};
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=296591 {ECO:0000313|EMBL:ABE46593.1, ECO:0000313|Proteomes:UP000001983};
RN   [1] {ECO:0000313|Proteomes:UP000001983}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500 {ECO:0000313|Proteomes:UP000001983};
RX   PubMed=18723656; DOI=10.1128/AEM.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(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 IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446}.
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DR   EMBL; CP000316; ABE46593.1; -; Genomic_DNA.
DR   RefSeq; WP_011485578.1; NC_007948.1.
DR   AlphaFoldDB; Q122E9; -.
DR   STRING; 296591.Bpro_4713; -.
DR   KEGG; pol:Bpro_4713; -.
DR   eggNOG; COG0550; Bacteria.
DR   eggNOG; COG5531; Bacteria.
DR   HOGENOM; CLU_002929_5_2_4; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000001983; 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-EC.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd10567; SWIB-MDM2_like; 1.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
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   InterPro; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
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; IPR005738; TopoIII.
DR   InterPro; IPR025589; Toprim_C_rpt.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   NCBIfam; TIGR01056; topB; 1.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13342; Toprim_Crpt; 2.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00151; SWIB; 1.
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; SSF47592; SWIB/MDM2 domain; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 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};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ABE46593.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001983};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          2..139
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   DOMAIN          916..992
FT                   /note="DM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51925"
FT   REGION          900..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   992 AA;  109023 MW;  67578940485BF069 CRC64;
     MKTLVIAEKP SVAQDIVRAI TPTAGKFEKH DEYFESDEWL VTSAVGHLVE IQAPEEFDVK
     RGKWSFANLP VIPPYFEVKP IDKTRTRLNA IVKLAKRKDV GAIVNACDAG REGELIFRLI
     QQYANSKHPV KRLWLQSMTP AAIREGFDSL RSEKQMQGLA DAARSRSEAD WMVGINGTRA
     MTAFNSRDGG FFLTTVGRVQ TPTLSVVVER EEKIRKFVSR DYWEIHASFL AEAGEYPAKW
     FDPKWKKAAA NADNAEPDAE LRADRVWSER EALAIAEAVR GKAATVTEES KPTTQAAGLL
     FDLTSLQREA NGKFGFSAKT TLSIAQSLYE RHKALTYPRT DSRALPEDYL PVVKQTFEML
     ADSGMRHLAP HAATAIKGNY IKPSKRIFDN AKVSDHFAII PTTQAPSGLS EAEQKLYDLV
     VRRFMAVFYP SAEYLVTTRI SQAVGYSFKT EGKVLVKPGW LAIYGKEAAD EVADAKDGDK
     GQSLVPVKPG EMVRAEVVEA KGLKTRPPAR YSEATLLGAM EGAGKTIDDD ELREAMQEKG
     LGTPATRAAT IEGLIAEKYM LREGRELIPT AKAFQLMTLL RGLGVEELSK AELTGEWEYK
     LAQMEHGKLS RETFMAEIAA MTENLVNKAK GYDKDTIPGD YTTLQTPCPN CGGVVKENYR
     RYTCTGKNGG DGCGFSFGKT PAGRTFETAE VEQFLRDRKI GPLEGFRSKA GWPFTAEMVI
     KFDEETKNYK LEFDFGDDKN GETGEIVDFG DQQSLGPCPR CAARVFELGK NYVCEKSVPT
     LEQPTPSCTF KTGQVILQQP IEREQMHKLL ETGKTDLLDK FVSMRTRRPF KAMLAWDKEA
     DKVNFEFAPS KFPPRKPAAA KTGVVKTPFG KTVAAKGAAG DAAPAAKKAA AKKVAAKKAP
     AKTAAPKVAR KAATPKPGAG LKPSDSLAAV IGAEPVARTQ VIKKLWDYIK AEGLQDAANK
     RAINADAKLL PVFGKPQVTM FELAGIVGKH LS
//
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