ID A0A1E8E0T3_9GAMM Unreviewed; 739 AA.
AC A0A1E8E0T3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 41.
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 ORFNames=BJN41_09155 {ECO:0000313|EMBL:OFE43207.1};
OS Acinetobacter towneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=202956 {ECO:0000313|EMBL:OFE43207.1, ECO:0000313|Proteomes:UP000186931};
RN [1] {ECO:0000313|EMBL:OFE43207.1, ECO:0000313|Proteomes:UP000186931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5-2Ac02 {ECO:0000313|EMBL:OFE43207.1,
RC ECO:0000313|Proteomes:UP000186931};
RA Barbosa B., Fernandez-Garcia L., Gato E., Leao R., Albano R., Fernandez B.,
RA Fernandez-Cuenca F., Marques E., Tomas M.;
RT "Genome of airborne Acinetobacter sp. 5-2Ac02 in the hospital environment:
RT Species near to Acinetobacter towneri.";
RL Submitted (OCT-2016) 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:OFE43207.1}.
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DR EMBL; MKQS01000015; OFE43207.1; -; Genomic_DNA.
DR RefSeq; WP_070154757.1; NZ_MKQS01000015.1.
DR STRING; 202956.BJN41_09155; -.
DR eggNOG; COG0188; Bacteria.
DR Proteomes; UP000186931; 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 12..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 425..454
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 43
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 79
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 123
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 739 AA; 82413 MW; F44F9D8C825D6AD1 CRC64;
MTSLAHHATE NRSVAEFTER AYLNYAMYVI MDRALPHISD GLKPVQRRIV YAXSXLGLKH
SGKPKKSART VGDVLGKYHP HGDSACYEAM VLMAQPFSYR YPFIEGQGNW GSPDDPKSFA
AMRYTEAKLS QYSEVLLAEL GQGTCDWQDN FDGSLKEPVN LPARVPNILL NGTTGIAVGM
ATDIPPHNLR EVVKGTIALI RNPNLTDEKV AEYIPAPDLP TKAEIITPPE ELLKMQSTGR
GSYRMRAVYS IEKNEIVITE LPYQVSGSKI ITQIADQMQA KKLPLVSDVR DESDHQNPTR
LVIVLRSNRI DAEAVMSHLF ATTDLESSYR VNMNMIGADG RPQVKSIRRI LLEWIEIRKN
TVTRRLQYHL NKIEKRLHIL AGLLIAYLDI DTVIRIIREE DHPKAELMAH FGIDEIQAEA
ILELKLRHLA KLEEMEIRRE QEELEARAAI IREQLANPES LKNLIISELK EDAKKFGDDR
RSPIVLRAEA TAINEQDMLP ADPVTVVLSE AGWIRCAKGH EVDAENLNFR AGDQYLSHAQ
GKSNQRVYIL DDTGRSYALP INSLPSARGL GEPLSSKLAP ASGVGFKQLL IADDEAEILA
VSSKGYGFKT QAKQLDTSAK AGKAFLSLPE QSTVMNLQMI EHASHVALLS SAGRLLVIEL
SELPILNKGK GNKLIQLEEK DQLVSMLPLS LDETIQVFAG QQQLKLKGDD LLKYVAKRGT
KGHLLPRGYQ KANKLLIQR
//
