ID E2SIW9_9FIRM Unreviewed; 832 AA.
AC E2SIW9;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 70.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00937};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00937};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00937};
GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00937,
GN ECO:0000313|EMBL:EFP62582.1};
GN ORFNames=HMPREF0983_00963 {ECO:0000313|EMBL:EFP62582.1};
OS Erysipelotrichaceae bacterium 3_1_53.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae.
OX NCBI_TaxID=658659 {ECO:0000313|EMBL:EFP62582.1, ECO:0000313|Proteomes:UP000006223};
RN [1] {ECO:0000313|EMBL:EFP62582.1, ECO:0000313|Proteomes:UP000006223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3_1_53 {ECO:0000313|EMBL:EFP62582.1,
RC ECO:0000313|Proteomes:UP000006223};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Pearson M., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA Walk T., White J., Yandava C., Allen-Vercoe E., Strauss J., Sibley C.,
RA Daigneault M., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Erysipelotrichaceae bacterium strain 3_1_53.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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_00937}.
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_00937};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC Rule:MF_00937}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00937};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00937}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_00937}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFP62582.1}.
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DR EMBL; ACTJ01000024; EFP62582.1; -; Genomic_DNA.
DR AlphaFoldDB; E2SIW9; -.
DR STRING; 658659.HMPREF0983_00963; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR Proteomes; UP000006223; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; cd00187; TOP4c; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR HAMAP; MF_00937; ParC_type2; 1.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR005741; TopoIV_A_Gpos.
DR NCBIfam; TIGR01061; parC_Gpos; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF9; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 5.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00937};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00937};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00937};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00937};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 17..469
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT ACT_SITE 128
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 48
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 84
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 86
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 97
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 103
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 127
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 832 AA; 94708 MW; 759830073C3CE1FE CRC64;
MKKKEQQLEH HSSVISSPLE EIMGDRFGRY SKYIIQDRAL PDARDGLKPV QRRILYAMYE
DGNTWDKGYR KSAKTVGLVI GNYHPHGDSS VYNAMVRMSQ EWKIRTPQID MQGNNGSIDD
DPAAAMRYTE ARLGKISEHL LKDIEKETVL WAPNFDDTAM EPTVLPARYP NLLVNGITGI
AAGYATNIPP HNLSEVIDAA VYRIQHADCS LEELMEYIQG PDFPTGGIVQ GLDGIREAFE
TGKGRIIVRG KAVIEQKKTV QQIVITEIPY EVVKSNMVKK IDDIRLNKKI EGILDVRDES
DRNGLRVVVD MKKDANGDVI LNYLYKNTDL QVSYNYNVVA IVDKRPVQMG LAQMLDAFIE
HRREVIERRS RYDLKKKEDR CHILEGLIKA VSILDEIIAL IRASKDKADS KRRIMDAFAF
SDAQAEAIVT MRLYRLSSTD ITQLREEYAT LLNEIEELHD ILENPRMLKK VMIRELHEVK
KAFKTPRLTR IEHEIEEIVI DKVAMINSEQ VMFTISRDGY FKRVSMRSYN AGKEDMTGLK
EGDHLVGYGE VNTLDHVLFF TTQGTYGYTP VYEVEESRWK EIGSHINSTI RISGEEKITD
AFVLRSFATN AYMISVTKNG LVKKTAVREY EVSRNNKTMS NMKLLEGDEV ITTMAAYDYD
EILIASKNGY VSRYPVSLIP ETSPRSKGVK AMNLVMDELV SACIHHADAS QLVVFTDQCQ
VKRIKLSDID VTGRPARGAM ICKKVKSKPY QIAHIALHEL NDELVIINEE TQKILAKDIS
LMSKDATFSS LLHATQEYYF LRTLVTVEQR ALTEQAAPDT TQEFEEIELF ED
//
