ID Q5E8Y9_VIBF1 Unreviewed; 805 AA.
AC Q5E8Y9;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 01-MAY-2013, entry version 73.
DE RecName: Full=DNA gyrase subunit B;
DE EC=5.99.1.3;
GN Name=gyrB; OrderedLocusNames=VF_0012;
OS Vibrio fischeri (strain ATCC 700601 / ES114).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium
RT with pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC stranded DNA in an ATP-dependent manner and also catalyzes the
CC interconversion of other topological isomers of double-stranded
CC DNA rings, including catenanes and knotted rings (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC of double-stranded DNA.
CC -!- COFACTOR: Magnesium. Binds two Mg(2+) per subunit. The magnesium
CC ions form salt bridges with both the protein and the DNA. Can also
CC accept other divalent metal cations, such as Mn(2+) and Ca(2+) (By
CC similarity).
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC Within the heterotetramer, GyrA contains the active site tyrosine
CC that forms a covalent intermediate with the DNA, while GyrB
CC contributes the cofactor binding sites and catalyzes ATP
CC hydrolysis (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC -!- SIMILARITY: Contains 1 Toprim domain.
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DR EMBL; CP000020; AAW84507.1; -; Genomic_DNA.
DR RefSeq; YP_203395.1; NC_006840.2.
DR ProteinModelPortal; Q5E8Y9; -.
DR SMR; Q5E8Y9; 10-393.
DR STRING; 312309.VF_0012; -.
DR EnsemblBacteria; AAW84507; AAW84507; VF_0012.
DR GeneID; 3279826; -.
DR KEGG; vfi:VF_0012; -.
DR PATRIC; 20110509; VBIVibFis127983_0013.
DR eggNOG; COG0187; -.
DR HOGENOM; HOG000075155; -.
DR KO; K02470; -.
DR OMA; IFETTEF; -.
DR ProtClustDB; PRK14939; -.
DR BioCyc; AFIS312309:GIWP-12-MONOMER; -.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:HAMAP.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR Gene3D; 3.40.50.670; -; 2.
DR HAMAP; MF_01898; GyrB; 1; -.
DR InterPro; IPR002288; DNA_gyrase_B_C.
DR InterPro; IPR011557; GyrB.
DR InterPro; IPR003594; HATPase_ATP-bd.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR013759; Topo_IIA_cen_dom.
DR InterPro; IPR013760; Topo_IIA_like_dom.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR006171; Toprim_domain.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00433; TOP2c; 1.
DR SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR TIGRFAMs; TIGR01059; gyrB; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Topoisomerase.
FT DOMAIN 419 534 Toprim (By similarity).
FT METAL 425 425 Magnesium 1; catalytic (By similarity).
FT METAL 499 499 Magnesium 1; catalytic (By similarity).
FT METAL 499 499 Magnesium 2 (By similarity).
FT METAL 501 501 Magnesium 2 (By similarity).
FT SITE 450 450 Interaction with DNA (By similarity).
FT SITE 453 453 Interaction with DNA (By similarity).
SQ SEQUENCE 805 AA; 89404 MW; 99E2F8CE31269448 CRC64;
MSENYDSSSI KVLKGLDAVR KRPGMYIGDT DDGTGLHHMV FEVVDNSIDE ALAGHCKDII
VTIHEDNSVS VSDDGRGIPT AIHPEEGVSA AEVIMTVLHA GGKFDDNSYK VSGGLHGVGV
SVVNALSEKV ELTIHRAGEI HQQVYHHGEP EAPLAVIGKT DTTGTKIRFW PSEETFTNVV
FVYEILAKRL RELSFLNSGV SIKLQDMREE DKADHFMYEG GIQAFVQHLN RNKTPIHQKV
FHFDSEREDG ISVEVSMQWN DGFQENIYCF TNNIPQRDGG THLAGFRSAL TRTLNTFMDK
EGFSKKAKAA TSGDDAREGL TAVVSVKVPD PKFSSQTKDK LVSSEVKSAV ESAMGEKLSE
FLAENPSEAK MVCSKIIDAA RAREAARKAR EMTRRKGALD IAGLPGKLAD CQEKDPGLSE
LYIVEGDSAG GSAKQGRNRK NQAILPLKGK ILNVEKARFD KMLSSQEVGT LITALGCGIG
RDEYNPDKLR YHNIIIMTDA DVDGSHIRTL LLTFFYRQMP ELIERGYIYI AQPPLYKVKK
GKQEQYIKDE DAMAEYQIAL ALDNASLFTN ADAPAIAGQA LEDLVVQYNS VMKLIDRMSR
RYPVSVLNRL VYTGRLTQEM CADEASAQAW TEAFVAELNA TEVGASQYNA ALLFDEEANA
YQPKLVVRTH GVEHEYVLSI DLLNSKEYAR IADLAEALDG LLEESAYAQR GERKQPVSSF
EDALAWLTKE SRRGFSLQRY KGLGEMNPEQ LWETTMDPES RRMMQVTIND AVAADELFTT
LMGDQVEPRR NFIEENALRV SNLDI
//
