ID E9LEY8_9NOCA Unreviewed; 408 AA.
AC E9LEY8;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:ADU56232.1};
OS Nocardia harenae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=358707 {ECO:0000313|EMBL:ADU56232.1};
RN [1] {ECO:0000313|EMBL:ADU56232.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL B-24459 {ECO:0000313|EMBL:ADU56232.1};
RA Everest G.J., Cook A.E., le Roes-Hill M., Meyers P.R.;
RT "Nocardia rhamnosiphila sp. nov., isolated from a compost heap.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000256|ARBA:ARBA00010708}.
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DR EMBL; HM856183; ADU56232.1; -; Genomic_DNA.
DR AlphaFoldDB; E9LEY8; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
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:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 252..366
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADU56232.1"
FT NON_TER 408
FT /evidence="ECO:0000313|EMBL:ADU56232.1"
SQ SEQUENCE 408 AA; 45089 MW; 6101A5A492793332 CRC64;
NKGLTIKLTD QRVTAEQVTA DEAGDTAEAP KQAEEAAAEQ TEHKVKTRTY HYPGGLEDFV
RHINRTKQPI HNSVVGFTGK GTGHELEVAM QWNSGYSESV HTFANTINTH EGGTHEEGFR
AALTTVVNRY AKDKKLLKEK DGNLTGDDIR EGLAAIVSVK VGEPQFEGQT KTKLGNTEVK
SFVQKTCNEH LQHWFEANPA DAKTIVQKAV SSAQARVAAR KARELVRRKS ATDLGGLPGK
LADCRSKDPQ KSEIYIVEGD SAGGSAKSGR DSMYQAILPI RGKIINVEKA RIDRVLKNNE
VQSIITAFGT GIHDEFDIAK LRYHKIVLMA DADVDGQHIS TLLLTLLFRF MRPLVEHGHV
YLAQPPLYKL KWQRGEAEFA YSDRERDGLL EAGLAAGKKI NKDDGIQR
//
