ID Q8VV26_9GAMM Unreviewed; 392 AA.
AC Q8VV26;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 89.
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:BAB83077.1};
OS Alcanivorax sp. Hak-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=146969 {ECO:0000313|EMBL:BAB83077.1};
RN [1] {ECO:0000313|EMBL:BAB83077.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Hak-2 {ECO:0000313|EMBL:BAB83077.1};
RA Kishira H., Ducrocq V., Harayama S.;
RT "Genetic diversity of Alcanivorax/Fundibacter, a taxonomic group comprising
RT petroleum-degrading marine bacteria.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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; AB053159; BAB83077.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VV26; -.
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 314..392
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAB83077.1"
FT NON_TER 392
FT /evidence="ECO:0000313|EMBL:BAB83077.1"
SQ SEQUENCE 392 AA; 43474 MW; AA6F7F4296E703D5 CRC64;
DDNTYKVSGG LHGVGVSVVN ALSEELKLTI RRNGQVHEQI YNHGVPAKPL EVVGTTDSSG
TAVHFRPSPE TFSNIKFHYD ILAKRLRELS FLNSGVRIHL MDERSGDEDV FEYEGGLSAF
VSYLNTNKTP LNQVFHFNYE REEDGIAVEV AMQWNDSYQE NIFCFTNNIP QRDGGTHLAG
FRAALTRTLN SYMDKEGFLK KEKASPSGDD AREGLTAVIS VKVPDPKFSS QTKDKLVSSE
VKSAVEQTMG DLFQDYLLEN PGEARSIVQK IIDAARARDA ARKAREMTRR KGALDIAGLP
GKLADCQQKD PALSELYIVE GDSAGGSAKQ GRDRKNQAIL PLKGKILNVE KARFDKMLSS
QEVGTLITAL GCGIGRDEYN IEKLRYHRII IM
//
