ID A0A077KR60_9FLAO Unreviewed; 629 AA.
AC A0A077KR60;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=CHSO_3012 {ECO:0000313|EMBL:BAP32049.1};
OS Chryseobacterium sp. StRB126.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=878220 {ECO:0000313|EMBL:BAP32049.1, ECO:0000313|Proteomes:UP000031650};
RN [1] {ECO:0000313|EMBL:BAP32049.1, ECO:0000313|Proteomes:UP000031650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StRB126 {ECO:0000313|EMBL:BAP32049.1,
RC ECO:0000313|Proteomes:UP000031650};
RX PubMed=25291777; DOI=10.1128/genomeA.00952-14;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Complete Genome Sequence of Chryseobacterium sp. Strain StRB126, an N-
RT Acylhomoserine Lactone-Degrading Bacterium Isolated from Potato Root.";
RL Genome Announc. 2:e00952-14(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR EMBL; AP014624; BAP32049.1; -; Genomic_DNA.
DR RefSeq; WP_045497833.1; NZ_AP014624.1.
DR AlphaFoldDB; A0A077KR60; -.
DR KEGG; chz:CHSO_3012; -.
DR HOGENOM; CLU_006146_1_1_10; -.
DR OrthoDB; 9802808at2; -.
DR Proteomes; UP000031650; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd01030; TOPRIM_TopoIIA_like; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR000565; Topo_IIA_B.
DR InterPro; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR PANTHER; PTHR45866:SF2; DNA TOPOISOMERASE (ATP-HYDROLYZING); 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:BAP32049.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 409..515
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
SQ SEQUENCE 629 AA; 72199 MW; B492EAEE742773A6 CRC64;
MSQEINPTYS EENIRTLDWQ EHIRLRPGMY IGKLGDGASA DDGIYILLKE ILDNSIDEFR
MRSGKRIEIK LDDGKVTIRD FGRGIPLGKM VDAVSKMNTG GKYDSKAFKK SVGLNGVGTK
AVNALSEYFR VRSFRDGMMK AAEFSRGMIK ENFDEKETSD RNGTEISFIP DGEIFLHFKY
RKEYIERMLR NYAYLNPGLK ILFNGETYFS ENGLKDLLEE ELESDILYPI VHLKDEDIEV
AITHSDKSQT ETYFSFVNGQ NTTQGGTHLN AFREAYVKTI REFFNKSFDA SDIRKSIIAA
ISINVEEPVF ESQTKTKLGS NDMGPNGPTV RTFIIDFLKS KLDNFLHKNP EIAEGIQRKI
LISERERKEL SGIQKLARER AKKVSLHNKK LRDCRQHYND QKAERKGDTQ IFITEGDSAS
GSITKSRDVE TQAVFSLKGK PLNCYGLTKK VVYENEEFNL LQAALNIEES LEDLRYNQVI
IATDADVDGM HIRLLMITFF LQFFPDLIKN NHLYILQTPL FRVRNKKETR YCYSEAERVK
ALNDLGKNPE ITRFKGLGEI SPDEFKHFIG KDIRLEPVVI GKDQTIDQLL EFYMGKNTPD
RQTFILENLV VEDDTDIDKK HILNEVSGQ
//
