ID GYRB_CAMJE Reviewed; 769 AA.
AC O87667; Q0PCC2; Q9PJA8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=DNA gyrase subunit B {ECO:0000255|HAMAP-Rule:MF_01898};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01898};
GN Name=gyrB {ECO:0000255|HAMAP-Rule:MF_01898}; OrderedLocusNames=Cj0003;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-714.
RC STRAIN=D450;
RA Misawa N., Allos B.M., Blaser M.J.;
RT "Differentiation of Campylobacter jejuni strains of serotype O19 from non-
RT O19 strains by polymerase chain reaction.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC Rule:MF_01898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01898};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01898};
CC Note=Binds two Mg(2+) per subunit. The magnesium ions form salt bridges
CC with both the protein and the DNA. Can also accept other divalent metal
CC cations, such as Mn(2+) or Ca(2+). {ECO:0000255|HAMAP-Rule:MF_01898};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-Rule:MF_01898}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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 topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC Rule:MF_01898}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC {ECO:0000255|HAMAP-Rule:MF_01898}.
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DR EMBL; AL111168; CAL34184.1; -; Genomic_DNA.
DR EMBL; AF093760; AAC62775.1; -; Genomic_DNA.
DR PIR; F81415; F81415.
DR RefSeq; WP_002858833.1; NZ_SZUC01000002.1.
DR RefSeq; YP_002343475.1; NC_002163.1.
DR AlphaFoldDB; O87667; -.
DR SMR; O87667; -.
DR IntAct; O87667; 1.
DR STRING; 192222.Cj0003; -.
DR PaxDb; 192222-Cj0003; -.
DR EnsemblBacteria; CAL34184; CAL34184; Cj0003.
DR GeneID; 904343; -.
DR KEGG; cje:Cj0003; -.
DR PATRIC; fig|192222.6.peg.3; -.
DR eggNOG; COG0187; Bacteria.
DR HOGENOM; CLU_006146_4_1_7; -.
DR OrthoDB; 9802808at2; -.
DR PHI-base; PHI:9791; -.
DR Proteomes; UP000000799; 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 (double strand cut, 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-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd16928; HATPase_GyrB-like; 1.
DR CDD; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR CDD; cd03366; TOPRIM_TopoIIA_GyrB; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_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 InterPro; IPR034160; TOPRIM_GyrB.
DR NCBIfam; TIGR01059; gyrB; 1.
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; PF00986; DNA_gyraseB_C; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR PRINTS; PR01159; DNAGYRASEB.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00387; HATPase_c; 1.
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; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..769
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000145301"
FT DOMAIN 414..528
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 445
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 448
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT CONFLICT 217
FT /note="E -> K (in Ref. 2; AAC62775)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="T -> I (in Ref. 2; AAC62775)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="D -> E (in Ref. 2; AAC62775)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="I -> V (in Ref. 2; AAC62775)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="Q -> P (in Ref. 2; AAC62775)"
FT /evidence="ECO:0000305"
FT CONFLICT 676..677
FT /note="RS -> IG (in Ref. 2; AAC62775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 769 AA; 86649 MW; B1BC8322F99C4F2D CRC64;
MQENYGASNI KVLKGLEAVR KRPGMYIGDT NIGGLHHMIY EVVDNSIDEA MAGHCDTIDV
EITTEGSCIV SDNGRGIPVD MHPTENMPTL TVVLTVLHAG GKFDKDTYKV SGGLHGVGVS
VVNALSKKLV ATVERNGEIY RQEFSEGKVI SEFGVIGKSK KTGTTIEFWP DDQIFEVTEF
DYEILAKRFR ELAYLNPKIT INFKDNRVGK HESFHFEGGI SQFVTDLNKK EALTKAIFFS
VDEEDVNVEV ALLYNDTYSE NLLSFVNNIK TPDGGTHEAG FRMGLTRVIS NYIEANASAR
EKDNKITGDD VREGLIAIVS VKVPEPQFEG QTKGKLGSTY VRPIVSKASF EYLTKYFEEN
PIEAKAIMNK ALMAARGREA AKKARELTRK KESLSVGTLP GKLADCQSKD PSESEIYLVE
GDSAGGSAKQ GRERSFQAIL PLRGKILNVE KARLDKILKS EQIQNMITAF GCGIGEDFDL
SKLRYHKIII MTDADVDGSH IQTLLLTFFF RFMNELVANG HIYLAQPPLY LYKKAKKQIY
LKDEKALSEY LIETGIEGLN YEGIGMNDLK DYLKIVAAYR AILKDLEKRF NVISVIRYMI
ENSNLVKGNN EELFSVIKQF LETQGHNILN HYINENEIRA FVQTQNGLEE LVINEELFTH
PLYEEASYIF DKIKDRSLEF DKDILEVLED VETNAKKGAT IQRYKGLGEM NPEQLWETTM
DPSVRRLLKI TIEDAQSAND TFNLFMGDEV EPRRDYIQAH AKDVKHLDV
//
