ID A0A1X9MAJ4_9BACI Unreviewed; 817 AA.
AC A0A1X9MAJ4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:ARK30455.1};
GN ORFNames=BkAM31D_11800 {ECO:0000313|EMBL:ARK30455.1};
OS Halalkalibacter krulwichiae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK30455.1, ECO:0000313|Proteomes:UP000193006};
RN [1] {ECO:0000313|EMBL:ARK30455.1, ECO:0000313|Proteomes:UP000193006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM31D {ECO:0000313|EMBL:ARK30455.1,
RC ECO:0000313|Proteomes:UP000193006};
RA Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL Submitted (APR-2017) 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; CP020814; ARK30455.1; -; Genomic_DNA.
DR RefSeq; WP_066151257.1; NZ_CP020814.1.
DR AlphaFoldDB; A0A1X9MAJ4; -.
DR STRING; 199441.BkAM31D_11800; -.
DR KEGG; bkw:BkAM31D_11800; -.
DR Proteomes; UP000193006; Chromosome.
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:UP000193006};
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..462
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 817 AA; 91964 MW; 1A4797A3A7D2A178 CRC64;
MAQSERYLDL PLEEVIGDRF GRYSKYIIQE RALPDARDGL KPVQRRILYA MYREGNTAEK
PFRKSAKTVG NVIGNYHPHG DSSVYEAMVR MSQEWKVRNL LVDMHGNNGS IDGDPPAAMR
YTEARLSKIA SQLLQDLDRD TVDFIPNFDD SEEEPVVLPS LYPNLLVNGS TGISAGYATD
IPPHHLGEII DGVIMQMEKP STTLDDLLTV IKGPDFPTGG IVQGIDGIRQ AYKTGKGKVV
VRAKTEIEEI RGGREQIVIT EIPYEVVKAN LVKKMDELRF DKKVDGIAEV RDDTDRTGLR
IVVELKKEAD AKAILNYLLK NTDLQVTYNF NMVAIANKAP KLMGLQTLIQ AYVDHQKIVF
TRRAKFDLKK ALDRQHIVRG LIKAISILDE VISTIRASRD KKDAKENLIA KFEFTEAQAE
AIVTLQLYRL TNTDITTLEE EAADLERRIH ELEAILSSEK KLISVIKKSL QLIKKEFADP
RRTLIKEEIE EIKINMDVLI ASEDVMVTVT KEGYVKRTSV RSYGASNGED PGMKEGDYLL
GHFELNTTET LLLFTKLGNY LYLPVHQLPD IRWKDNGQHV ANLVSGLDRE DEIIKALPIK
EFKEEESLLF ITKNGMAKRS QLSLYQAQRF SKPLMAIKLK EGDEVVTMMH TSGKNDLFIA
THLGYGLWLT EEEINLVGQR AAGVKAINLK EGDAVVGAAT FSPEDKKVEF MVVTQRGAVK
KVPITEFDKS SRAKRGLVML RELKSNPHRV IACKKVTNQA STFTLRTKND VIESFAAGNY
RNSDRYSNGS FIVDVATKGE VVEVWEVIDT TIKTDEQ
//
