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Database: UniProt
Entry: Q5NDK1_9GAMM
LinkDB: Q5NDK1_9GAMM
Original site: Q5NDK1_9GAMM 
ID   Q5NDK1_9GAMM            Unreviewed;       372 AA.
AC   Q5NDK1;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 76.
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:CAI34862.1};
OS   Aeromonas sp. V32.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=305866 {ECO:0000313|EMBL:CAI34862.1};
RN   [1] {ECO:0000313|EMBL:CAI34862.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=V32 {ECO:0000313|EMBL:CAI34862.1};
RA   Kupfer M., Kuhnert P., Korczak B.M., Peduzzi R., Demarta A.;
RT   "Genetic relationships of Aeromonas strains inferred from 16S rRNA, gyrB
RT   and rpoB gene sequences.";
RL   Int. J. Syst. Evol. Microbiol. 56:2743-2751(2006).
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; AJ868364; CAI34862.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5NDK1; -.
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          303..372
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAI34862.1"
FT   NON_TER         372
FT                   /evidence="ECO:0000313|EMBL:CAI34862.1"
SQ   SEQUENCE   372 AA;  41029 MW;  A9E35E8A97C0F3C0 CRC64;
     HGVGVSVVNA LSDKLLLTIR RNGHVYEQTY HLGEPQAPLK 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 ARFDKMISSQ EVGTLITALG
     CGIGRDEYNP DK
//
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