(data stored in ACNUC7421 zone)

SWISSPROT: A8FP49_SHESH

ID   A8FP49_SHESH            Unreviewed;       813 AA.
AC   A8FP49;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 82.
DE   RecName: Full=DNA gyrase subunit B {ECO:0000256|HAMAP-Rule:MF_01898, ECO:0000256|SAAS:SAAS00746468};
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=Ssed_0009 {ECO:0000313|EMBL:ABV34622.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34622.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34622.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34622.1,
RC   ECO:0000313|Proteomes:UP000002015};
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., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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;
CC         Evidence={ECO:0000256|SAAS:SAAS00609977};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00709652};
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}.
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DR   EMBL; CP000821; ABV34622.1; -; Genomic_DNA.
DR   ProteinModelPortal; A8FP49; -.
DR   STRING; 425104.Ssed_0009; -.
DR   EnsemblBacteria; ABV34622; ABV34622; Ssed_0009.
DR   KEGG; sse:Ssed_0009; -.
DR   eggNOG; ENOG4105C7D; Bacteria.
DR   eggNOG; COG0187; LUCA.
DR   HOGENOM; HOG000075155; -.
DR   KO; K02470; -.
DR   OMA; DCSSRDP; -.
DR   OrthoDB; POG091H01XP; -.
DR   Proteomes; UP000002015; 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-KW.
DR   GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP.
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; 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   InterPro; IPR034160; TOPRIM_GyrB.
DR   PANTHER; PTHR10169; PTHR10169; 1.
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; 2.
DR   TIGRFAMs; TIGR01059; gyrB; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FP49.
DR   SWISS-2DPAGE; A8FP49.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00528655};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01898};
KW   DNA-binding {ECO:0000256|SAAS:SAAS00709661};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01898,
KW   ECO:0000256|SAAS:SAAS00107007, ECO:0000313|EMBL:ABV34622.1};
KW   Magnesium {ECO:0000256|SAAS:SAAS00058309};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00058330};
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      427    542       Toprim. {ECO:0000259|PROSITE:PS50880}.
SQ   SEQUENCE   813 AA;  90888 MW;  08342774B2937649 CRC64;
     MNNRRENNMS ENSYDSSSIK VLKGLDAVRK RPGMYIGDTD DGTGLHHMVF EVVDNSIDEA
     LAGHCNDVII TIHADGSVSV KDDGRGIPVA IHPEEGISAA EVIMTVLHAG GKFDDNSYKV
     SGGLHGVGVS VVNALSHKLQ LTIRRDGKLY EQFYTHGEPD EPIKAIGDAT NTGTEIRFWP
     STDTFTDVLF HFDILAKRVR ELSFLNSGVG VRLVDERDNR DEFFKYDGGI SAFVDYLNVN
     KTPVNKEVFH FIQERDDGIT VEVAMQWNDG FQENIFCFTN NIPQRDGGTH LAGFRGALTR
     NLNTYMEREG YNKKGKTGAT GDDAREGLTA VISVKVPDPK FSSQTKDKLV SSEVKSAVEQ
     TMGEQLGDYL MEHPNEAKLI VGKIIDAARA REAARKAREM TRRKGALDLG GLPGKLADCQ
     EKDPALSEIY IVEGDSAGGS AKQGRNRKNQ AILPLKGKIL NVEKARFDKM LSSQEVATLI
     TALGCGIGRD EYDPDKTRYH NIVIMTDADV DGSHIRTLLL TFFFRQMPEL IERGFVYIAQ
     PPLYKVKKGK QEQYLKDDPA LTEFLTNLAL DGGEIHASAN APAMSGAPLE KLVYQYREVE
     AIFDRLDQRY PLMLTERMLY HPALSNDVLA DEAKVQQWCD AYVADLAEKE SGGYIFSGEA
     FLEPERQVYL PKITIRKHGI DTHYLFSYDF LQSSDYERMA KLATALDGLI EEGGYVKRGE
     RLKEVSSFVE ALDWLMNDSR RGLYIQRYKG LGEMNPEQLW ETTMDPESRR MLVVTIEDAI
     AADQLFTCLM GDQVEPRREF IESNALNVAN LDV
//

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