GYRB_MYCBP
ID GYRB_MYCBP Reviewed; 714 AA.
AC A0A0G2Q9D6;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 1.
DT 03-AUG-2022, entry version 31.
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=gyrB1 {ECO:0000255|HAMAP-Rule:MF_01898}; OrderedLocusNames=BCG_0005;
GN and
GN Name=gyrB2 {ECO:0000255|HAMAP-Rule:MF_01898}; OrderedLocusNames=BCG_0035;
OS Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=410289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Pasteur 1173P2;
RX PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA Barrell B.G., Parkhill J., Cole S.T.;
RT "Genome plasticity of BCG and impact on vaccine efficacy.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN [2]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBUNIT, AND REACTION MECHANISM.
RC STRAIN=BCG / ATCC 27289 / DSM 43990;
RX PubMed=7503546; DOI=10.1006/abbi.1995.9919;
RA Wu L.C., Shahied S.I.;
RT "Mycobacterial DNA gyrase: enzyme purification and characterization of
RT supercoiling activity.";
RL Arch. Biochem. Biophys. 324:123-129(1995).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded DNA in an ATP-dependent manner and also
CC catalyzes the interconversion of other topological isomers of double-
CC stranded DNA rings, including catenanes and knotted rings. Relaxes
CC negatively supercoiled DNA in an ATP-independent manner. A linear
CC reaction intermediate can be trapped in the presence of the antibiotic
CC ciprofloxacin (PubMed:7503546). Negative supercoiling favors strand
CC separation, and DNA replication, transcription, recombination and
CC repair, all of which involve strand separation. Type II topoisomerases
CC break and join 2 DNA strands simultaneously in an ATP-dependent manner.
CC {ECO:0000269|PubMed:7503546}.
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 ECO:0000269|PubMed:7503546};
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 -!- ACTIVITY REGULATION: DNA supercoiling is inhibited by EDTA, novobiocin,
CC coumermycin and ciprofloxacin (PubMed:7503546).
CC {ECO:0000269|PubMed:7503546}.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:7503546). In the heterotetramer, GyrA contains the active site
CC tyrosine that forms a transient covalent intermediate with DNA, while
CC GyrB binds cofactors and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-
CC Rule:MF_01898, ECO:0000269|PubMed:7503546}.
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; AM408590; CAL69989.1; -; Genomic_DNA.
DR EMBL; AM408590; CAL70019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2Q9D6; -.
DR SMR; A0A0G2Q9D6; -.
DR KEGG; mbb:BCG_0005; -.
DR KEGG; mbb:BCG_0035; -.
DR HOGENOM; CLU_006146_4_1_11; -.
DR OMA; LWETTMH; -.
DR Proteomes; UP000001472; 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:0034335; F:DNA negative supercoiling activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Magnesium; Metal-binding;
KW Nucleotide-binding; Topoisomerase.
FT CHAIN 1..714
FT /note="DNA gyrase subunit B"
FT /id="PRO_0000435541"
FT DOMAIN 492..606
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 498
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 571
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 571
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT BINDING 573
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 523
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
FT SITE 526
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01898"
SQ SEQUENCE 714 AA; 78456 MW; 39497519D7191365 CRC64;
MGKNEARRSA LAPDHGTVVC DPLRRLNRMH ATPEESIRIV AAQKKKAQDE YGAASITILE
GLEAVRKRPG MYIGSTGERG LHHLIWEVVD NAVDEAMAGY ATTVNVVLLE DGGVEVADDG
RGIPVATHAS GIPTVDVVMT QLHAGGKFDS DAYAISGGLH GVGVSVVNAL STRLEVEIKR
DGYEWSQVYE KSEPLGLKQG APTKKTGSTV RFWADPAVFE TTEYDFETVA RRLQEMAFLN
KGLTINLTDE RVTQDEVVDE VVSDVAEAPK SASERAAEST APHKVKSRTF HYPGGLVDFV
KHINRTKNAI HSSIVDFSGK GTGHEVEIAM QWNAGYSESV HTFANTINTH EGGTHEEGFR
SALTSVVNKY AKDRKLLKDK DPNLTGDDIR EGLAAVISVK VSEPQFEGQT KTKLGNTEVK
SFVQKVCNEQ LTHWFEANPT DSKVVVNKAV SSAQARIAAR KARELVRRKS ATDIGGLPGK
LADCRSTDPR KSELYVVEGD SAGGSAKSGR DSMFQAILPL RGKIINVEKA RIDRVLKNTE
VQAIITALGT GIHDEFDIGK LRYHKIVLMA DADVDGQHIS TLLLTLLFRF MRPLIENGHV
FLAQPPLYKL KWQRSDPEFA YSDRERDGLL EAGLKAGKKI NKEDGIQRYK GLGEMDAKEL
WETTMDPSVR VLRQVTLDDA AAADELFSIL MGEDVDARRS FITRNAKDVR FLDV
