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Database: UniProt
Entry: Q60AM8_METCA
LinkDB: Q60AM8_METCA
Original site: Q60AM8_METCA 
ID   Q60AM8_METCA            Unreviewed;       628 AA.
AC   Q60AM8;
DT   23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=DNA topoisomerase 4 subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
DE            EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00938};
DE   AltName: Full=Topoisomerase IV subunit B {ECO:0000256|HAMAP-Rule:MF_00938};
GN   Name=parE {ECO:0000256|HAMAP-Rule:MF_00938,
GN   ECO:0000313|EMBL:AAU93104.1};
GN   OrderedLocusNames=MCA0820 {ECO:0000313|EMBL:AAU93104.1};
OS   Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylococcus.
OX   NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU93104.1, ECO:0000313|Proteomes:UP000006821};
RN   [1] {ECO:0000313|EMBL:AAU93104.1, ECO:0000313|Proteomes:UP000006821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC   {ECO:0000313|Proteomes:UP000006821};
RX   PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA   Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA   Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA   Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA   Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA   Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA   Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA   Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT   "Genomic insights into methanotrophy: the complete genome sequence of
RT   Methylococcus capsulatus (Bath).";
RL   PLoS Biol. 2:1616-1628(2004).
CC   -!- FUNCTION: Topoisomerase IV is essential for chromosome segregation. It
CC       relaxes supercoiled DNA. Performs the decatenation events required
CC       during the replication of a circular DNA molecule. {ECO:0000256|HAMAP-
CC       Rule:MF_00938}.
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         ECO:0000256|HAMAP-Rule:MF_00938};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC       Rule:MF_00938}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family. ParE type 1
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00938}.
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DR   EMBL; AE017282; AAU93104.1; -; Genomic_DNA.
DR   RefSeq; WP_010960144.1; NC_002977.6.
DR   AlphaFoldDB; Q60AM8; -.
DR   STRING; 243233.MCA0820; -.
DR   KEGG; mca:MCA0820; -.
DR   eggNOG; COG0187; Bacteria.
DR   HOGENOM; CLU_006146_1_0_6; -.
DR   OMA; RDGKTHH; -.
DR   Proteomes; UP000006821; Chromosome.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd16928; HATPase_GyrB-like; 1.
DR   CDD; cd00822; TopoII_Trans_DNA_gyrase; 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   HAMAP; MF_00938; ParE_type1; 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; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR005737; TopoIV_B_Gneg.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   NCBIfam; TIGR01055; parE_Gneg; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   PANTHER; PTHR45866:SF4; DNA TOPOISOMERASE 4 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; PR01098; TOPISMRASE4B.
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|HAMAP-Rule:MF_00938};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00938};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00938};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006821};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00938}.
FT   DOMAIN          412..525
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   BINDING         5
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         69
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         110..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   BINDING         334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            446
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            497
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
FT   SITE            615
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00938"
SQ   SEQUENCE   628 AA;  69214 MW;  F26B9205B975CC1B CRC64;
     MNEVYDASAI EVLSGLDPVR RRPGMYTDTT RPDHLAQEVI DNAVDEALAG FARLIEIRLL
     ADGGLEVRDD GRGMPVDIHP ELGVSGVEVI LTRLHAGGKF SRKAYRYSGG LHGVGVSVVN
     ALSLRLEVEV RRDGKVHAIA FEKGEKVGDL TETGTTPRRA TGTTVRFWPE AHYFDNARFS
     RSRLKHLLRA KAVLCPGLEI RMTDDASGET ETWCYRNGLP QYLLDQLQGC ACIPDEPFTG
     AMEGRQEAVE WAVLWCPEGA APVAESYVNL VPTVQGGTHV NGLRTGLTEA VREFCEYRNL
     LPRGIKIVPD DVWERCNHVL SVKMQEPQFA GQTKERLNSR ECASFVSGVV KDAFSLWLNQ
     HPAVGERIAE LVIESAQKRL RAARRVTRKK VSSGPALPGK LADCAAQDVN RTELFLVEGD
     SAGGSAKQAR DKDFQAIMPL RGKILNTWEV ESGAILASQE VHDISLAIGV DPGATDLSGL
     RYGKICVLAD ADSDGNHIAT LLCALFLRHF RALVKAGHVF IAMPPLYRID VGKQVYYALD
     EAEKKGVLDR IEAEKIKGKV NVLRFKGLGE MNPVQLRETT MNPDTRRLVQ LSLDDAAATD
     ERLDMLLAKR RAGDRRVWLE EKGNLADI
//
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