ID D3Y4C9_9GAMM Unreviewed; 352 AA.
AC D3Y4C9;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:ADD12312.1};
OS Isoalcanivorax pacificus W11-5.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Isoalcanivorax.
OX NCBI_TaxID=391936 {ECO:0000313|EMBL:ADD12312.1};
RN [1] {ECO:0000313|EMBL:ADD12312.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=W11-5 {ECO:0000313|EMBL:ADD12312.1};
RX PubMed=20584816; DOI=10.1099/ijs.0.022368-0;
RA Lai Q., Wang L., Liu Y., Fu Y., Zhong H., Wang B., Chen L., Wang J.,
RA Sun F., Shao Z.;
RT "Alcanivorax pacificus sp. nov., isolated from a deep-sea pyrene-degrading
RT consortium.";
RL Int. J. Syst. Evol. Microbiol. 61:1370-1374(2011).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GU395984; ADD12312.1; -; Genomic_DNA.
DR AlphaFoldDB; D3Y4C9; -.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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 293..352
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADD12312.1"
FT NON_TER 352
FT /evidence="ECO:0000313|EMBL:ADD12312.1"
SQ SEQUENCE 352 AA; 38981 MW; E349BC55647F8476 CRC64;
ALSEELKLTI RRNGKVHEQV YRHGVPNEPL KVVGETEGTG TTVRFRPSAA TFTNIKFHYD
ILAKRLRELS FLNSGVRIHL KDERTGQEDL FEYEGGLSAF VAYLNGAKTP LNRVFHFQCD
REDGIGVEVA LQWNDSYNEN IYCFTNNIPQ RDGGAHLAGF RAALTRTLNS YMENEGFLKK
EKVATTGDDA REGLTAVISV KVPDPKFSSQ TKDKLVSSEV KTAVEQTMSE LFQDYLLENP
AEAKQIVQKI IDAARARDAA RKAREMTRRK GALDIAGLPG KLADCQEKDP ALSELYLVEG
DSAGGSAKQG RDRRTQAILP LKGKILNVEK ARFDKMLSSQ EVGTLITALG CG
//