GYRB_MYCGA
ID GYRB_MYCGA Reviewed; 648 AA.
AC P47720;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, 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=MYCGA7240;
GN ORFNames=MGA_0616;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S6;
RX PubMed=7557470; DOI=10.1016/0378-1119(95)00440-h;
RA Forsyth M.H., Sayed A.S., Geary S.J.;
RT "Sequence and transcriptional analysis of the genes encoding the class-II
RT topoisomerase of Mycoplasma gallisepticum.";
RL Gene 163:161-162(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; U18306; AAA57341.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP57074.1; -; Genomic_DNA.
DR RefSeq; WP_011113987.1; NC_004829.2.
DR AlphaFoldDB; P47720; -.
DR SMR; P47720; -.
DR PRIDE; P47720; -.
DR KEGG; mga:MGA_0616; -.
DR PATRIC; fig|233150.7.peg.814; -.
DR HOGENOM; CLU_006146_4_1_14; -.
DR OMA; LWETTMH; -.
DR OrthoDB; 205481at2; -.
DR Proteomes; UP000001418; 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; 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;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..648
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000145318"
FT DOMAIN 433..547
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 439
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 512
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 512
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 514
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 464
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 467
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT CONFLICT 154
FT /note="P -> S (in Ref. 1; AAA57341)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="S -> N (in Ref. 1; AAA57341)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> S (in Ref. 1; AAA57341)"
FT /evidence="ECO:0000305"
FT CONFLICT 301..310
FT /note="FKNALYKIIN -> LRMLFIRSY (in Ref. 1; AAA57341)"
FT /evidence="ECO:0000305"
FT CONFLICT 430..431
FT /note="ME -> G (in Ref. 1; AAA57341)"
FT /evidence="ECO:0000305"
FT CONFLICT 605
FT /note="T -> I (in Ref. 1; AAA57341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 648 AA; 73713 MW; E14AD95ED11117BB CRC64;
MNNTKKDQYS SQSIKVLEGL SAVRKRPGMY IGSTDQKGLH HMIWEIIDNS VDEMMAGYGT
TVKLTLKDNY LVEVEDDGRG IPVDIHEKTN KSTVETVLTI LHAGGKFDSD TYSMSGGLHG
VGASVVNALS SSFKVWVNRD YKIHYIEFKD GGVPLKPLEI IGTDSKKQGT RIQFVPDFSI
MEQFEYDETI IADRIEQLAF LNKGIKFIFN DERTDKKTKQ EWLYEGGIKQ YVENLNASKE
PIIPQIIYGE KKTKVTLPKR NLEVTMLLEV AFQYTNGYYN STYSFCNNIH TNQGGTHEEG
FKNALYKIIN RYALEKKFIK ETDGKISKED LSEGLTAIIS IKHSEPQYQG QTKDRLGNTE
VREFTNSVVS ELLERFFLEN PEEAAKITAK AVSAMFSRKR SEAALESARK SPFESASLPG
KLADCTTKDM EISELYIVEG DSAGGSAKSG RDRFYQAILP LRGKVLNVEK ANHEKIFKNE
EIRTLITAIG AGVNPEFSLD KIRYNKIIIM TDADVDGAHI RILLLTFFFR HMFPLIEKGH
VYIAQPPLYR VSYNKQNKYI YSDAQLEEWK NQNPNVRYEL QRYKGLGEMD DVQLWETTMD
PEKRTLLKVS INDAANADKT FSLLMGDEVS PRRDFIEKNA KSVKNIDF
