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Database: UniProt
Entry: Q6XDE6_9GAMM
LinkDB: Q6XDE6_9GAMM
Original site: Q6XDE6_9GAMM 
ID   Q6XDE6_9GAMM            Unreviewed;       321 AA.
AC   Q6XDE6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 80.
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:AAP69921.1};
OS   Aeromonas sp. P1W-98.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=234695 {ECO:0000313|EMBL:AAP69921.1};
RN   [1] {ECO:0000313|EMBL:AAP69921.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P1W-98 {ECO:0000313|EMBL:AAP69921.1};
RX   PubMed=15388703; DOI=10.1099/ijs.0.03048-0;
RA   Soler L., Yanez M.A., Chacon M.R., Aguilera-Arreola M.G., Catalan V.,
RA   Figueras M.J., Martinez-Murcia A.J.;
RT   "Phylogenetic analysis of the genus Aeromonas based on two housekeeping
RT   genes.";
RL   Int. J. Syst. Evol. Microbiol. 54:1511-1519(2004).
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; AY237563; AAP69921.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6XDE6; -.
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          283..321
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAP69921.1"
FT   NON_TER         321
FT                   /evidence="ECO:0000313|EMBL:AAP69921.1"
SQ   SEQUENCE   321 AA;  35568 MW;  61725D982B9D0B3A CRC64;
     RNGHVYEQTY HLGEPHAPLK QIGDSSSGTG TEVRFWPSPT IFTDTLYHYE ILAKRLRELS
     FLNSGVSIRL QDERDGREVH FCYEGGIKAF VEYLNQNKTP IHPKVFHFST EQDGIGVEVA
     MQWNDAYQEG VYCFTNNIPQ RDGGTHLVGF RTALTRTLNT YMDKEDYSKK AKSAASGDDV
     REGLIAVISV KVPDPKFSSQ TKDKLVSSEV KTAVEQAMGE KLGEFLLENP GDAKIVVNKI
     IDAARAREAA RKARELTRRK GALDIAGLPG KLADCQEKDP ALSELYIVEG DSAGGSAKQG
     RNRKNQAILP LKGKILNVEK A
//
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