ID F8V7P1_9NOCA Unreviewed; 160 AA.
AC F8V7P1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:AEH94593.1};
OS Nocardia exalbida.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=290231 {ECO:0000313|EMBL:AEH94593.1};
RN [1] {ECO:0000313|EMBL:AEH94593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44883 {ECO:0000313|EMBL:AEH94593.1};
RX PubMed=20844218; DOI=10.1128/JCM.00883-10;
RA McTaggart L.R., Richardson S.E., Witkowska M., Zhang S.X.;
RT "Phylogeny and identification of Nocardia species on the basis of
RT multilocus sequence analysis.";
RL J. Clin. Microbiol. 48:4525-4533(2010).
RN [2] {ECO:0000313|EMBL:AEH94593.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44883 {ECO:0000313|EMBL:AEH94593.1};
RA McTaggart L.R., Richardson S.E., Witkowska M., Zhang S.X.;
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AMK09110.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CNM20070400 {ECO:0000313|EMBL:AMK09110.1};
RX PubMed=27148228; DOI=10.3389/fmicb.2016.00542;
RA Carrasco G., de Dios Caballero J., Garrido N., Valdezate S., Canton R.,
RA Saez-Nieto J.A.;
RT "Shortcomings of the Commercial MALDI-TOF MS Database and Use of MLSA as an
RT Arbiter in the Identification of Nocardia Species.";
RL Front. Microbiol. 7:542-542(2016).
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; JN041241; AEH94593.1; -; Genomic_DNA.
DR EMBL; KT933524; AMK09110.1; -; Genomic_DNA.
DR AlphaFoldDB; F8V7P1; -.
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 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 PRINTS; PR01159; DNAGYRASEB.
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.
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 1..102
FT /note="DNA topoisomerase type IIA subunit B"
FT /evidence="ECO:0000259|Pfam:PF00204"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AEH94593.1"
FT NON_TER 160
FT /evidence="ECO:0000313|EMBL:AEH94593.1"
SQ SEQUENCE 160 AA; 17300 MW; B83AEFBEDB921BB5 CRC64;
LTTVVNKYAK DKRLIKEKDG NLTGDDIREG LAAIVSVKVG EPQFEGQTKT KLGNTEVKSF
VQRTCNEHLT HWFEANPADA KTIVNKAVSS AQARVAARKA RELVRRKSAT DLGGLPGKLA
DCRSKDPSKS EIYIVEGDSA GGSAKSGRDS MYQAILPLRG
//
