ID C5GZT7_ALILO Unreviewed; 395 AA.
AC C5GZT7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 57.
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:ABY62585.1};
OS Aliivibrio logei (Vibrio logei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=688 {ECO:0000313|EMBL:ABY62585.1};
RN [1] {ECO:0000313|EMBL:ABY62585.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WHSW18 {ECO:0000313|EMBL:ABY62590.1}, and WHSW4
RC {ECO:0000313|EMBL:ABY62585.1};
RX PubMed=19481895; DOI=10.1016/j.syapm.2009.04.005;
RA Ast J.C., Urbanczyk H., Dunlap P.V.;
RT "Multi-gene analysis reveals previously unrecognized phylogenetic diversity
RT in Aliivibrio.";
RL Syst. Appl. Microbiol. 32:379-386(2009).
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; EU185875; ABY62585.1; -; Genomic_DNA.
DR EMBL; EU185880; ABY62590.1; -; Genomic_DNA.
DR AlphaFoldDB; C5GZT7; -.
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 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.
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 316..395
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABY62585.1"
FT NON_TER 395
FT /evidence="ECO:0000313|EMBL:ABY62585.1"
SQ SEQUENCE 395 AA; 43695 MW; 4CCF254F0483B127 CRC64;
DDNSYKVSGG LHGVGVSVVN ALSEKVELTI NRRGEIFQQI YCHGVPQAPL AVIGTTDTTG
TKIRFWPSDQ TFANIEFVYD ILAKRLRELS FLNSGVSIRL QDMREEDKSD HFMFEGGIKA
FVTHLNRNKT PVHQKIFYFD AERKEDGIVV EVAMQWNDSY QENIFCYTNN IPQRDGGAHL
SGFRSALTRT LNSFMDKEGF SKKAKSSASG DDAREGLTAV VSVKVPDPKF SSQTKDKLVS
SEVKSAVESA MNEKLAEFLA ENPGEAKMVC SKIIDAARAR EAARKAREMT RRKGALDIAG
LPGKLADCQE KDPAQSELYI VEGDSAGGSA KQGRNRKNQA ILPLKGKILN VEKARFDKMI
SSQEVGTLIT ALGCGIGRDE YNPDKLRYHN IIIMT
//
