ID A7YLZ5_SALBN Unreviewed; 391 AA.
AC A7YLZ5;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=DNA gyrase subunit B {ECO:0000256|ARBA:ARBA00019166};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE Flags: Fragment;
GN Name=gyrB {ECO:0000313|EMBL:ABU96759.1};
OS Salmonella bongori.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=54736 {ECO:0000313|EMBL:ABU96759.1};
RN [1] {ECO:0000313|EMBL:ABU96759.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 13772 {ECO:0000313|EMBL:ABU96759.1};
RA Chang H.-W., Nam Y.-D., Jung M.Y., Kim K.-H., Roh S.W., Oh H.-M.,
RA Yoon J.-H., Jeon C.-O., Bae J.-W.;
RT "Comparison of Genome-Probing Microarrays to Conventional DNA-DNA
RT Hybridization Methods.";
RL Submitted (JUL-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU014645; ABU96759.1; -; Genomic_DNA.
DR AlphaFoldDB; A7YLZ5; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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: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 Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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: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; 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 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 313..391
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABU96759.1"
FT NON_TER 391
FT /evidence="ECO:0000313|EMBL:ABU96759.1"
SQ SEQUENCE 391 AA; 43421 MW; 72FD230374620DAE CRC64;
DNSYKVSGGL HGVGVSVVNA LSQKLELVIQ RDGKIHRQIY EHGVPQAPLA VTGDTDKTGT
MVRFWPSLET FTNVTEFEYE ILAKRLRELS FLNSGVSIRL RDKRDGKEDH FHYEGGIKAF
VEYLNKNKTP IHPNIFYFST EKDGIGVEVA LQWNDGFQEN IYCFTNNIPQ RDGGTHLAGF
RAAMTRTLNA YMDKEGYSKK AKVSATGDDA REGLIAVVSV KVPDPKFSSQ TKDKLVSSEV
KSAVEQQMNE LLSEYLLENP SDAKIVVGKI IDAARAREAA RRAREMTRRK GALDLAGLPG
KLADCQERDP ALSELYLVEG DSAGGSAKQG RNRKNQAILP LKGKILNVEK ARFDKMLSSQ
EVATLITALG CGIGRDEYNP DKLRYHSIII R
//
