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Database: UniProt
Entry: Q936C1_SERFO
LinkDB: Q936C1_SERFO
Original site: Q936C1_SERFO 
ID   Q936C1_SERFO            Unreviewed;       323 AA.
AC   Q936C1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 82.
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:CAC69419.1};
OS   Serratia fonticola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:CAC69419.1};
RN   [1] {ECO:0000313|EMBL:CAC69419.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CIP 78.64T {ECO:0000313|EMBL:CAC69419.1};
RX   PubMed=11931166;
RA   Dauga C.;
RT   "Evolution of the gyrB gene and the molecular phylogeny of
RT   Enterobacteriaceae: a model molecule for molecular systematic studies.";
RL   Int. J. Syst. Evol. Microbiol. 52:531-547(2002).
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; AJ300539; CAC69419.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q936C1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          119..288
FT                   /note="DNA topoisomerase type IIA subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF00204"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAC69419.1"
FT   NON_TER         323
FT                   /evidence="ECO:0000313|EMBL:CAC69419.1"
SQ   SEQUENCE   323 AA;  36226 MW;  0FD785623B87CFBA CRC64;
     KFDDNSYKVS GGLHGVGVSV VNALSEKLEL VIRREGKVHE QTYKHGEPQA PLKVVGETDQ
     TGTTLRFWPS FQTFTNNIEF EYDILAKRLR ELSFLNSGVS IRLKDKRNDR EDHFHYEGGI
     RAFVEYLNKN KTPIHPNVFY FSTVKDDIGV EVALQWNDGF QENIYCFTNN IPQRDGGTHL
     AGFRAAMTRT LNTYMDKEGY SKKSKISATG DDAREGLIAV VSVKVPDPKF SSQTKDKLVS
     SEVKTAVESL MNEKLVDYLM ENPADAKIVV GKIIDAARAR EAARKAREMT RRKGALDLAG
     LPGKLADCQE RDPALSELYL VEG
//
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