ID A0A143YAM2_9LACT Unreviewed; 821 AA.
AC A0A143YAM2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=Tpal_588 {ECO:0000313|EMBL:CZQ85105.1};
OS Trichococcus palustris.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=140314 {ECO:0000313|EMBL:CZQ85105.1, ECO:0000313|Proteomes:UP000242754};
RN [1] {ECO:0000313|EMBL:CZQ85105.1, ECO:0000313|Proteomes:UP000242754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus palustris {ECO:0000313|EMBL:CZQ85105.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-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_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; FJNE01000002; CZQ85105.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143YAM2; -.
DR STRING; 140314.SAMN04488076_10172; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000242754; 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:UP000242754};
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..455
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 821 AA; 92667 MW; 2B407892EDC6E201 CRC64;
MTDNQEIKEI MLEDVMGDRF GRYSKYIIQD RALPDIRDGL KPVQRRILYA MFVAGNTSEK
GFRKSAKTVG NVIGNYHPHG DSSVYEAMVR LSQDWKMREE LIEMHGNNGS MDGDSAAAMR
YTEARLSKIS AELLRDIDKE TVDFVLNFDD TDEEPTVLPA KYPNLLVNGA TGISAGYATD
IPPHNLGEVI DATLHLISHP DATLADLMKY VKGPDFPTGA MIQGLEGLKD AYTTGKGKVI
VRSKTRIEEI RGGKQQIIIS EIPYEINKAT LVKKMDDIRI NRKIEGISEV RDESDRTGLQ
IVVELKKEAN AEGILNYLLK NTDLQVNYNF NMVAIDERRP KQVGLHQILK AYVKYQKEVI
TRRTKYNLKK AEARLHIVDA LIKVISILDE VIQIIRNSKD KKDSKQNLIK SYAFTEIQAE
AIVSLQLYRL SNTDITALQN EKMDLNEQVA MYQSILKDDK TLYSVMKNEL TAVKKQYANP
RRSSVQAEID EIKIDTEVLV PDEEVIVVVT KEGYYKRTSV RSFSASAIEE VALREGDKPL
FIGKASTLDA VVLFTNKGDY LHFPIHELPE LKWKDIGHHL SQNIPFAADE RIISVTIMKH
HTEATGTVLF VSQDGLIKQT NLNEFTTFRG YRNKKSVAMK MKNETDAIVS LHYLDEKTNY
EILLATHFGF ALRYPVSEVP TIGTRASGVK SINLKTGDFV VGGAVFTEQN EDYPILIITQ
RGNIKRFKSG EVPPLGRAKR GLMLLKELKA KPHRIIYMDS SLEQPNTYII HTTNGADIQA
ESKEVPFSPR YANGSFAINE KTDGEVTSVE KAYNFSQIRI L
//
