(data stored in ACNUC7421 zone)

SWISSPROT: C8VVA2_DESAS

ID   C8VVA2_DESAS            Unreviewed;       635 AA.
AC   C8VVA2;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898};
DE            EC=5.6.2.3 {ECO:0000256|HAMAP-Rule:MF_01898};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898};
GN   OrderedLocusNames=Dtox_0006 {ECO:0000313|EMBL:ACV60971.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV60971.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV60971.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: A type II topoisomerase that negatively supercoils
CC       closed circular double-stranded (ds) DNA in an ATP-dependent
CC       manner to modulate DNA topology and maintain chromosomes in an
CC       underwound state. Negative supercoiling favors strand separation,
CC       and DNA replication, transcription, recombination and repair, all
CC       of which involve strand separation. Also able to catalyze the
CC       interconversion of other topological isomers of dsDNA rings,
CC       including catenanes and knotted rings. Type II topoisomerases
CC       break and join 2 DNA strands simultaneously in an ATP-dependent
CC       manner. {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898, ECO:0000256|SAAS:SAAS01180974};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00924966};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00888357};
CC   -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC       In the heterotetramer, GyrA contains the active site tyrosine that
CC       forms a transient covalent intermediate with DNA, while GyrB binds
CC       cofactors and catalyzes ATP hydrolysis. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC       negative supercoils. Not all organisms have 2 type II
CC       topoisomerases; in organisms with a single type II topoisomerase
CC       this enzyme also has to decatenate newly replicated chromosomes.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01898}.
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; CP001720; ACV60971.1; -; Genomic_DNA.
DR   RefSeq; WP_012813423.1; NC_013216.1.
DR   STRING; 485916.Dtox_0006; -.
DR   EnsemblBacteria; ACV60971; ACV60971; Dtox_0006.
DR   KEGG; dae:Dtox_0006; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075155; -.
DR   KO; K02470; -.
DR   OMA; IYIACPP; -.
DR   OrthoDB; 205481at2; -.
DR   BioCyc; DACE485916:G1GFV-6-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   HAMAP; MF_01898; GyrB; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
DR   InterPro; IPR011557; GyrB.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
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   InterPro; IPR034160; TOPRIM_GyrB.
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   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8VVA2.
DR   SWISS-2DPAGE; C8VVA2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924926}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00888349};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924998, ECO:0000313|EMBL:ACV60971.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00906748};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00906804};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924952};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00924964}.
FT   DOMAIN      420    534       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   COILED      383    403       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   635 AA;  71416 MW;  50C55CA12E96FDC3 CRC64;
     MPERITERYG AEEIQVLEGL EAVRRRPGMY IGSTGAKGLH HLVYEVVDNS IDEAMAGYCD
     HIEVFINEDN SITVTDNGRG IPVDIHSKTG NSAVELVMTT LHAGGKFGGG GYKVSGGLHG
     VGVSVVNALS KWLEVEVRRQ GKIFFQRYER GIPVSDLKIV GDSSFTGTKI TFSPDEEIFE
     DVIFSRETLE QRLQELAYLN SRVKIYLKDF INNLEFSYMY EGGIKDFVAH INQDKILLPE
     APLYFVREKD HVMVEVAMQY TDAYFENLFS YVNNIHTIDG GTHEAGFRSA LTRVINDYAK
     KNNLIKNNEG NLSGEDIREG LTAVISIKVP EPQFEGQTKG KLGNSEVRGI VDSVVAEGLS
     TFLEENPAVS KKIIEKSISA FRAREAARKA RELTRRKNVL ESSTLPGKLS DCSNRDPSES
     ELYLVEGDSA GGSAKQGRDR KFQAILPLKG KILNVEKARL DKILNNDEIR AMITALGTGI
     GEDFDITKAR YHKLIIMTDA DVDGSHIRTL LLTFFYRYMR PLIEAGYIFI AQPPLYRLKK
     GKMEIYLYSD RDLENKLKEV GRNGISIQRY KGLGEMDAQQ LWDTTMDPEN RTILMVELEN
     AAEADKIFDT LMGDRVEPRR SFINKHAHDV RNLDI
//

If you have problems or comments...

PBIL Back to PBIL home page