ID A0A0U1NZ20_9BACI Unreviewed; 812 AA.
AC A0A0U1NZ20;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
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:CRK83284.1};
GN ORFNames=BN000_03247 {ECO:0000313|EMBL:CRK83284.1};
OS Neobacillus massiliamazoniensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1499688 {ECO:0000313|EMBL:CRK83284.1, ECO:0000313|Proteomes:UP000199087};
RN [1] {ECO:0000313|Proteomes:UP000199087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LF1 {ECO:0000313|Proteomes:UP000199087};
RA Urmite Genomes;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CVRB01000003; CRK83284.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1NZ20; -.
DR STRING; 1499688.BN000_03247; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199087; 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; TIGR01063; gyrA; 1.
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}; Coiled coil {ECO:0000256|SAM:Coils};
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 Reference proteome {ECO:0000313|Proteomes:UP000199087};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 10..463
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 428..495
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 41
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 79
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 96
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 120
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 812 AA; 91671 MW; 371BCA715863B9B7 CRC64;
MSPTEKFRDL PLEDVLGDRF GRYSKYIIQE RALPDARDGL KPVQRRILYA MHVEGNTHDK
GFRKSAKTVG NVIGNYHPHG DSSVYEAMVR MSQDWKVRNV LVEMHGNNGS VDGDPPAAMR
YTEARLSAIA AELLRDIEKQ TVEFIPNFDD TSKEPTVLPA MFPNLLVNGS TGISAGYATD
IPPHHLGEVI DGVILKMDQP DASVEELMKV VKGPDFPTGG IIQGIDGIKK AYETGKGKII
IRSKADIEEM RGGKQQIVIT EIPYEVNKAN LVKKIDEFRL DRKVEGISEV RDETDRTGLR
IVIELKKEAD AAGVLTFLYK NSDLQVAYNF NMVAIHNKRP KLMGLRELLD AYIEHQKEVV
TKRTRFELNK AKERQHIVEG LMKALSILDE VIATIRASKD KRDAKDNLIA KFAFTELQAE
AIVSLQLYRL TNTDITALRN EAEELAQKIE EWTSILASEK KLFSVIKKEL KDVKKRFADN
RRSRIEAEIE ELKINLEVMV PSEDVIVTVT KHGYVKRTSQ RSYAASNGQD LAMKDSDRLL
AQLDMNTKDV LLLFTNKGNY LFCPVHELPD IRWKDLGQHV ANIIAIERDE EIIKAIPVKD
FETDSFLVFI TKNGMVKKTE LKAYKAQRYS KSLVAINLKD DDQVIDVHMT DGTIELFLIS
QLGYSLWFDE EEISIVGIRA AGVKGMNLKD DDFVVGGKII DPTSDDTIVI ATQRGSIKRM
KLKEFEKTSR AKRGVVILRE LKSNPHRVVG FLTAKESDSI VVQTEKGFTE SIRTANIRFS
DRYSNGSFIL DEGDNGKVTT IWKEEAPEKP SE
//
