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Database: UniProt
Entry: B6V6Y5_AERME
LinkDB: B6V6Y5_AERME
Original site: B6V6Y5_AERME 
ID   B6V6Y5_AERME            Unreviewed;       283 AA.
AC   B6V6Y5;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   27-MAR-2024, entry version 59.
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:ACJ06173.1};
OS   Aeromonas media.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=651 {ECO:0000313|EMBL:ACJ06173.1};
RN   [1] {ECO:0000313|EMBL:ACJ06173.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ER.1.18 {ECO:0000313|EMBL:ACJ06178.1}, ER.1.19
RC   {ECO:0000313|EMBL:ACJ06179.1}, and ER.1.8
RC   {ECO:0000313|EMBL:ACJ06173.1};
RX   PubMed=22127350; DOI=10.1016/j.resmic.2011.10.010;
RA   Moura A., Pereira C., Henriques I., Correia A.;
RT   "Novel gene cassettes and integrons in antibiotic-resistant bacteria
RT   isolated from urban wastewaters.";
RL   Res. Microbiol. 163:92-100(2012).
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; FJ238495; ACJ06173.1; -; Genomic_DNA.
DR   EMBL; FJ238500; ACJ06178.1; -; Genomic_DNA.
DR   EMBL; FJ238501; ACJ06179.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6V6Y5; -.
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; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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          81..250
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACJ06173.1"
FT   NON_TER         283
FT                   /evidence="ECO:0000313|EMBL:ACJ06173.1"
SQ   SEQUENCE   283 AA;  31566 MW;  27A83D222E919B61 CRC64;
     VYEQTYHLGE PQAPLKQIGD STGTGTEVRF WPSPTIFTDT LYHYEILAKR LRELSFLNSG
     VSIRLMDERD GREAHFCYEG GIKAFVEYLN QNKTPIHPKV FHFTTEQDGI GVEVAMQWND
     AYQEGVYCFT NNIPQRDGGT HLVGFRTALT RTLNSYMDKE DYSKKAKSAA SGDDVREGLI
     AVISVKVPDP KFSSQTKDKL VSSEVKTAVE QAMGEKLADF LLENPGDAKI VVNKIIDAAR
     AREAARKARE LTRRKGALDI AGLPGKLADC QEKDPALSEL YIV
//
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