ID A6XM66_SALET Unreviewed; 323 AA.
AC A6XM66;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 63.
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:ABI96415.1};
OS Salmonella enterica subsp. enterica serovar Panama.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=29472 {ECO:0000313|EMBL:ABI96415.1};
RN [1] {ECO:0000313|EMBL:ABI96415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=10676_02 {ECO:0000313|EMBL:ABI96415.1};
RA Sandjong B.T., Sessitsch A., Liebana E., Kornschober C., Allerberger F.,
RA Hachler H., Stralis-Pavese N., Bodrossy L.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABI96415.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=10676_02 {ECO:0000313|EMBL:ABI96415.1};
RA Tankouo-Sandjong B., Sessitsch A., Stralis-Pavese N., Liebana E.,
RA Kornschober C., Allerberger F., Hachler H., Bodrossy L.;
RT "Development of an oligonucleotide microarray method for Salmonella
RT serotyping.";
RL Microb. Biotechnol. 1:513-522(2008).
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; DQ838375; ABI96415.1; -; Genomic_DNA.
DR AlphaFoldDB; A6XM66; -.
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 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 265..323
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABI96415.1"
FT NON_TER 323
FT /evidence="ECO:0000313|EMBL:ABI96415.1"
SQ SEQUENCE 323 AA; 35871 MW; 674C7B77CA83225E CRC64;
LAVTGDTDKT GTMVRFWPSH ETFTNVTEFE YEILAKRLRE LSFLNSGVSI RLRDKRDGKE
DHFHYEGGIK AFVEYLNKNK TPIHPNIFYF STEKDGIGVE VALQWNDGFQ ENIYCFTNNI
PQRDGGTHLA GFRAAMTRTL NAYMDQEGYS KKAKVSATGD DAREGLIAVV SVKVPDPKFS
SQTKDKLVSS EVKSAVEQQM NELLSEYLLE NPSDAKIVVG KIIDAARARE AARRAREMTR
RKGALDLAGL PGKLADCQER DPALSELYLV EGDSAGGSAK QGRNRKNQAI LPLKGKILNV
EKARFDKMLS SQEVATLITA LGC
//
