ID A0A368X7I1_9BACI Unreviewed; 815 AA.
AC A0A368X7I1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=DFR57_11654 {ECO:0000313|EMBL:RCW63775.1};
OS Saliterribacillus persicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Saliterribacillus.
OX NCBI_TaxID=930114 {ECO:0000313|EMBL:RCW63775.1, ECO:0000313|Proteomes:UP000252585};
RN [1] {ECO:0000313|EMBL:RCW63775.1, ECO:0000313|Proteomes:UP000252585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27696 {ECO:0000313|EMBL:RCW63775.1,
RC ECO:0000313|Proteomes:UP000252585};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RCW63775.1}.
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DR EMBL; QPJJ01000016; RCW63775.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368X7I1; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000252585; 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}; 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:UP000252585};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 8..461
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 426..460
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 39
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 75
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 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 94
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 815 AA; 92884 MW; 0519ED970C7596A7 CRC64;
MEEKFLDLPL EEVIGDRFGR YSKYIIQDRA LPDARDGLKP VQRRILYAMH MERNTFEKPF
RKSAKTVGVV IGNYHPHGDS SVYEAMVRLS MTWKVRNVLV EMHGNNGSVD GDPPAAMRYT
EARLSAISSE LIRDIEKETV EFIPNFDDSI NEPVVLPARF PNLLANGSTG ISAGYATEIP
PHNLGEVIDA VIKMIDNPAI EIDELIKIIK GPDFPTGGII QGLEGLKKAY KTGRGKIIVR
GKASIEKLKS SREQIVIDEI PYEVNKAVLV KRMDELRLDR KVEGIAEVRD ETDRTGMRIV
IELKKDADSE GILHYLYKNT DLQIAYHFNM VAIKDKTPTL LNLTDILEAY ISHQKEVVTR
QTRFDLRKAQ ERAHIVEGLI KAISVLDELI KTIRASNDKQ DAKERIIKKY DFSDRQAEAI
VNLQLYRLTN TDITALEGEA SELREQITGY EEILANEKKL LSVIKKDLKL MKKKYADKRQ
TQIEEKIEEL KINLEVMVAS EDVLVSVTRD GYLKRTSLRS YGASTDADFT IKDQDHLVAL
LEINTTENIL LFTNKGRYVI VPVHQLPDIK WKDLGQHVSN LASLEKNEKI VKVIPVQEFK
KDEYLIFFTA NGMVKKSSLE VYSSQRFARP LIAINLKGED ELLNVHLSNG NADIFVATNT
GYGLWFHESE VAVIGQRASG VKAIQLKKDE KVVNGLIFDD LIKEQQFILV TQRGACKRMD
LSRFEKSSRA KRGLIMLREL KRNTHRVVGF DIVNEEEMIE FSTTKDVLKR FSPVELPKSD
RYSNGSFMID TDQHGEVKEV WKTATYRQPF TNENI
//
