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Database: UniProt
Entry: D3Y4C9_9GAMM
LinkDB: D3Y4C9_9GAMM
Original site: D3Y4C9_9GAMM 
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}.
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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
//
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