ID I3DMA4_HAEPH Unreviewed; 746 AA.
AC I3DMA4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_00936};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000256|HAMAP-Rule:MF_00936};
GN Name=parC {ECO:0000256|HAMAP-Rule:MF_00936,
GN ECO:0000313|EMBL:EIJ72847.1};
GN ORFNames=HMPREF1050_0100 {ECO:0000313|EMBL:EIJ72847.1};
OS Haemophilus parahaemolyticus HK385.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=1095744 {ECO:0000313|EMBL:EIJ72847.1, ECO:0000313|Proteomes:UP000003016};
RN [1] {ECO:0000313|EMBL:EIJ72847.1, ECO:0000313|Proteomes:UP000003016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK385 {ECO:0000313|EMBL:EIJ72847.1,
RC ECO:0000313|Proteomes:UP000003016};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (FEB-2012) 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_00936}.
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_00936};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000256|HAMAP-
CC Rule:MF_00936}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00936};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00936}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_00936}.
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:EIJ72847.1}.
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DR EMBL; AJSW01000008; EIJ72847.1; -; Genomic_DNA.
DR RefSeq; WP_005705668.1; NZ_UGHI01000002.1.
DR AlphaFoldDB; I3DMA4; -.
DR GeneID; 78223353; -.
DR PATRIC; fig|1095744.4.peg.438; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000003016; 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_00936; ParC_type1; 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; IPR005742; TopoIV_A_Gneg.
DR NCBIfam; TIGR01062; parC_Gneg; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 2.
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|HAMAP-Rule:MF_00936};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00936};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00936};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00936};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 14..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 429..457
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 124
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 45
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 81
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 83
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 746 AA; 82818 MW; F1E3CAC83A3DA418 CRC64;
MSNTIINYEG VEQMPIKRFT EDAYLNYSMY VIMDRALPFI GDGLKPVQRR IIYAMSELGL
NANAKYAKAA RTVGDVLGKF HPHGDSACYG AMVGMAQDFT FRYPLIDGQG NWGSLEDDAA
AYRYTEARLT KFSSVLLSEI DQGTVDFKPN FDGSKIEPVT FPSRLPHILL NGSTGIAVGM
ATDIPPHNIN ELADACVMLL DNPNATLTDI LSVVQGPDYP TLAEIITPKS EIVKIYEQGR
GSIKARAVWQ KEDGKIVINA LPYQTSPSKI IEQIAAQMKN KKLPMVDDVR DESNHENPIR
IVIIPRSNRI DFNALMDHLF ATTELEKSFR INMNMIGLDG KPAVKNLHTI LTEWLSFRRA
TVTRRLNYRL DKILDRLHII EGLIIAFLSI NEVIEIIRNE DEPKATLMAR FGLSEIQADA
ILNLRLRNLA KLEETTLKAE QNALEKERDE LQVLLGSERR LNTLIKKEIQ TDAKTFASPR
SSIFVERAEA KAISEADLTP TEDVTVILSE KGWVRCAKGH DIDVKGLAYR AGDQYLAHAH
GRSNQPVVFL DSTGRAYTID PISLPSARSQ GEPLTSKITL PEGAEIQQVL MGQPTENVLM
ASNSGYGFLC TFEDLISRNK AGKAVISLTE NAKTLPPQLV SLEEKCSLVA ISNVGRMLVF
PLSELPTLSK GKGNKIINIS AQAAKAGEEY LAHLLLLKPN QSLVFVSGKR KITLKPADIE
KYRGERARKG TQVRGLNEHS IIEILD
//
