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Database: UniProt/TrEMBL
Entry: A8LVH4_SALAI
LinkDB: A8LVH4_SALAI
Original site: A8LVH4_SALAI 
ID   A8LVH4_SALAI            Unreviewed;       648 AA.
AC   A8LVH4;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   11-MAY-2016, entry version 72.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00555050};
DE            EC=5.99.1.3 {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00470646};
GN   Name=gyrB {ECO:0000256|HAMAP-Rule:MF_01898};
GN   OrderedLocusNames=Sare_0007 {ECO:0000313|EMBL:ABV95943.1};
OS   Salinispora arenicola (strain CNS-205).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=391037 {ECO:0000313|EMBL:ABV95943.1, ECO:0000313|Proteomes:UP000001153};
RN   [1] {ECO:0000313|EMBL:ABV95943.1, ECO:0000313|Proteomes:UP000001153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNS-205 {ECO:0000313|EMBL:ABV95943.1,
RC   ECO:0000313|Proteomes:UP000001153};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S.,
RA   Penn K., Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.;
RT   "Complete sequence of Salinispora arenicola CNS-205.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA. {ECO:0000256|HAMAP-Rule:MF_01898,
CC       ECO:0000256|SAAS:SAAS00470725}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01898};
CC       Note=Binds two Mg(2+) per subunit. The magnesium ions form salt
CC       bridges with both the protein and the DNA. Can also accept other
CC       divalent metal cations, such as Mn(2+) or Ca(2+).
CC       {ECO:0000256|HAMAP-Rule:MF_01898};
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   -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000256|HAMAP-
CC       Rule:MF_01898}.
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DR   EMBL; CP000850; ABV95943.1; -; Genomic_DNA.
DR   RefSeq; WP_012180256.1; NC_009953.1.
DR   ProteinModelPortal; A8LVH4; -.
DR   STRING; 391037.Sare_0007; -.
DR   EnsemblBacteria; ABV95943; ABV95943; Sare_0007.
DR   GeneID; 5707580; -.
DR   KEGG; saq:Sare_0007; -.
DR   PATRIC; 23428419; VBISalAre38676_0007.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075154; -.
DR   KO; K02470; -.
DR   OMA; IKNMITA; -.
DR   OrthoDB; EOG6P334W; -.
DR   BioCyc; SARE391037:GH66-7-MONOMER; -.
DR   Proteomes; UP000001153; 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-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
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; 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.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013759; Topo_IIA_cen_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; 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;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001153};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01898};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00470744, ECO:0000313|EMBL:ABV95943.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00445358};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00445373};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528653};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528650}.
FT   DOMAIN      425    539       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   METAL       431    431       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       504    504       Magnesium 1; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_01898}.
FT   METAL       504    504       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   METAL       506    506       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01898}.
FT   SITE        456    456       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
FT   SITE        459    459       Interaction with DNA. {ECO:0000256|HAMAP-
FT                                Rule:MF_01898}.
SQ   SEQUENCE   648 AA;  72001 MW;  8775535031C910BD CRC64;
     MAAQDKQEYG AESITVLEGL EAVRKRPGMY IGSTGERGLH HLVWEVVDNA VDEALAGYCD
     TIDVVLLADG GVRVTDNGRG FPVDPHPKLK KPGVEVALTV LHAGGKFDGK AYAVSGGLHG
     VGVSVVNALS TRMAVEIQKD GYFWRQSYTD SKPSPLEKGE PTDATGSAVS FWPDPAVFET
     VDFDFQTIYR RLQEMAFLNR GLTIHFLDER VAADEDGKMR EVTFCYKGGI ADFVRHLNAS
     KTPIHKSVVE FGTEEDGMSV EIAMQWNESY GESVYTFANN INTHEGGTHE EGFRAALTSV
     INRYGADKRL LKSDEKLSGE DIREGLAAII SVKLTNPQFE GQTKTKLGNT PVKSFVQRVC
     NEWLVDWLDR NPAEAKVIIT KASQAARARV AAQQARKLAR RKSLLESGSM PGKLADCQST
     DPRECEVFIV EGDSAGGSAK QGRDPRTQAI LPIRGKILNV EKARIDRVLK NNEVQALITA
     LGTGIHDDFD IEKLRYHKIV LMADADVDGQ HIQTLLLTLL FRFMRPLVEL GHVYLAAPPL
     YKIKWNRKGD DAQYAYSDRE RDGLIALRQQ KKPNAKPDDI QRFKGLGEMN YPELWETTMN
     PATRTLRQVT LDDAATADEL FSVLMGEDVE ARRSFIQRNA KDVRFLDI
//
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