ID A0A2Z6TAT5_9LACO Unreviewed; 827 AA.
AC A0A2Z6TAT5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:GBG05063.1};
GN ORFNames=LrDSM24759_09770 {ECO:0000313|EMBL:GBG05063.1};
OS Lactobacillus rodentium.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=947835 {ECO:0000313|EMBL:GBG05063.1, ECO:0000313|Proteomes:UP000257317};
RN [1] {ECO:0000313|Proteomes:UP000257317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24759 {ECO:0000313|Proteomes:UP000257317};
RA Tanizawa Y., Tohno M., Endo A., Arita M.;
RT "New taxa in the Lactobacillus gasseri group.";
RL Submitted (MAR-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:GBG05063.1}.
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DR EMBL; BFBY01000006; GBG05063.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6TAT5; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000257317; 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; 3.
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:UP000257317};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00937}.
FT DOMAIN 11..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 429..456
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 42
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 78
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 80
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 97
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
FT SITE 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00937"
SQ SEQUENCE 827 AA; 93273 MW; 5FAFA6F115AB7435 CRC64;
MADTVERIKE LPLEEVMGER FGRYSKYIIQ ERALPDVRDG LKPVQRRILY AMYKDNNTYD
KPYKKAAKAV GNVMGNFHPH GDSSIYGALV HLSQEWKMRE PLIEMHGNNG SMDGDGPAAM
RYTESRLSKI SNLLLQDIDK DTVPMILNFD DTEYEPTVLP SHFPNLLVNG STGISAGYAT
EIPPHNLAEV IDAAVYLLKN PEANTDDLMQ FVKGPDFPTG GIVLGKKGIK EAYETGRGRI
QVRSKTSIQD IKGHRQQIVV TEIPFGVNKA MMVKKIDEIR LNKEIDGIAE VRDETDRHGL
SIVIELKKGA DSQNILNYLF KNTDLQISYN FNMVAIDHMA PVQVSLKKIL SSYLEHKKEV
VTKRTEFDLG KAKQRLEIVE GLIHALDILD QVIKTIRASK DKKDAKNNLI KEFDFTPNQA
EAIVSLQLYR LTNTDVNQLK AEQADLNEKI ATYEDILNNQ DVLEKVVVKE LNQVKKDFGS
PRRTEITEKA AKIEINEKAL VADETVRVLV SRDGYLKRSS LRSYQSTDET DNGLPAGDEV
IFEKTMSTLS NLYLFTNKGN LIYRPVHELV ETKWKETGQH LSQELGLAQD EEIIRVFEIN
DLKATDNFLL ATNDGYIKQV ALADLQPTRT YKSRAIIAMK LKKSDSKVVR VDRIKADSKQ
EITLITNQAY AIRYDIDEIP TSGARAAGVK SVNLKDEDYI VDYVLASPDT VDEIKIGLIT
QRGAFKQLEL NIINKVTRAK RGVMVLRELK TKPHRISAVS SYGQNHELIL TTSSQRQVKI
DTNNYPLGDR YSNGSFVLDP TTDGRPISLK LGKVLTNEKD DVSNLFE
//
