GenomeNet

Database: UniProt
Entry: H6N5Y5_MYCHN
LinkDB: H6N5Y5_MYCHN
Original site: H6N5Y5_MYCHN 
ID   H6N5Y5_MYCHN            Unreviewed;       657 AA.
AC   H6N5Y5;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   Name=gyrB {ECO:0000313|EMBL:AEW44900.2};
GN   OrderedLocusNames=MHC_00170 {ECO:0000313|EMBL:AEW44900.2};
OS   Mycoplasma haemocanis (strain Illinois).
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=1111676 {ECO:0000313|EMBL:AEW44900.2, ECO:0000313|Proteomes:UP000009135};
RN   [1] {ECO:0000313|EMBL:AEW44900.2, ECO:0000313|Proteomes:UP000009135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Illinois {ECO:0000313|EMBL:AEW44900.2,
RC   ECO:0000313|Proteomes:UP000009135};
RX   PubMed=22374945; DOI=10.1128/JB.06781-11;
RA   do Nascimento N.C., Guimaraes A.M., Santos A.P., Sanmiguel P.J.,
RA   Messick J.B.;
RT   "Complete genome sequence of Mycoplasma haemocanis strain Illinois.";
RL   J. Bacteriol. 194:1605-1606(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003199; AEW44900.2; -; Genomic_DNA.
DR   AlphaFoldDB; H6N5Y5; -.
DR   STRING; 1111676.MHC_00170; -.
DR   KEGG; mhe:MHC_00170; -.
DR   HOGENOM; CLU_006146_4_1_14; -.
DR   Proteomes; UP000009135; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd16928; HATPase_GyrB-like; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR002288; DNA_gyrase_B_C.
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   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 {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AEW44900.2};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009135};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          440..555
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
SQ   SEQUENCE   657 AA;  74047 MW;  4F737644C44F0EFF CRC64;
     MESTGNDPED LGQKGNYTDS SIKVLEGLEA VRERPGMYIG STDSKGLHHL IWEVLDNSVD
     EVLAGHANEV VLTLKPDHVI SINDNGRGIP TGINPQTNIS NLITVFTILH AGGKFDNNSY
     KTSGGLHGVG STCVNALSEF MEVTVCRNGE EHFVSFKNGG KIDKEPTLVS KVPVEKTGTR
     VTWKPDFSIF DKSDYDIGLI ETRLERLAYL NKGRKFVFDN QISKEVKEFF FKDGISDWVK
     NLNNSRKAIN DVIFLKEDGT VKNRRSPDIQ NPISISCAFQ YTLGDSPIVY SFCNNIYTAS
     GGTHLESFKD GILSCIRERS LEAKLIKESI DLVKSDILAG LTAIVSLNYS NPEYSGQTKE
     VLSNIEIKSF IREKVEELFG RFLEENSDQC KAILQRVDQE RNLRLKVEMA RQTDRKLALE
     GFMSFAGKLA DCTTKSVDFS ELYVVEGDSA GGSAKSARNR EYQAILPIKG KLLNVWKKTN
     TSSIVENEEI KSLISSIGCA YGDKFDKEKL RYNKVIIMTD ADVDGSHIRI LLLTFIYRFM
     RPLIEEGHVY IAQPPLYRAF TNKEVVYLFD DKKKDEFMAD KGKSKSWEIS RFKGLGEMSP
     EQLWQTTMNP EERIICKVTV EDMEQVTGIF DDLMGKKVHP RTEFILANYS NIRNLDI
//
DBGET integrated database retrieval system