ID A0A1I4ZEQ9_9NEIS Unreviewed; 795 AA.
AC A0A1I4ZEQ9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN05660284_01610 {ECO:0000313|EMBL:SFN48752.1};
OS Formivibrio citricus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Formivibrio.
OX NCBI_TaxID=83765 {ECO:0000313|EMBL:SFN48752.1, ECO:0000313|Proteomes:UP000242869};
RN [1] {ECO:0000313|Proteomes:UP000242869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6150 {ECO:0000313|Proteomes:UP000242869};
RA Varghese N., Submissions S.;
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}.
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DR EMBL; FOVE01000010; SFN48752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4ZEQ9; -.
DR STRING; 83765.SAMN05660284_01610; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000242869; 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; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000242869};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_00936}.
FT DOMAIN 47..519
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 484..514
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 158
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 78
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 114
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 116
FT /note="Interaction with DNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
FT SITE 157
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00936"
SQ SEQUENCE 795 AA; 87133 MW; BF965370702F6CF7 CRC64;
MTQEFEPQEL NLAEEVTEAD PPVADDGGNL RYIQAQISSE PGDGESVQLG LYAEKSYLEY
AMSVVKSRAL PQVEDGQKPV QRRILFAMHG LGLTAGAKPM KSARIVGDVL GKYHPHGDQS
AYDALVRIAQ DFSLRYPLID GHGNFGSRDG DGAAAYRYTE ARLTPIAELL LSEIDKGTTD
FIPNYDGAFE EPVLLPARLP VLLLNGATGI AVGMATEVPS HNLGEVADAA VALIRNPELS
TADLMSYIPG PDLPGGGQII SAARDIQNAY ETGRGSLKLR ARWEKEDLAR GQWQIVVTQL
PQGASAQKVL EEIEELTNPK VKKGKKALSQ DQLQTKQLIL SVLDRVRDES GKDCPVRLVF
EPKSSRQNPD ELMTLLLANT SLETNLPINM VMIGRDGRPA QKSLKTLLSE WIDFRFVTVT
RRTRHRLGQV NDRIHILEGR LIVFLNIDEV IRIIRESDEP KAALIARFNL SDRQAEDILE
IRLRQLARLE GIKLEQELSD LRKEKDDLEH LLANPSAMQK LVVKEIEADR KKYADPRRTL
IEEAERAVVE VAVVDEPTTI ILSDKGWLRS RQGHGIDLQS LAFKDGDKLL AAIECRTVDQ
IALFGSDGRV YTIAASSVPG GRGDGVPVTT LVDLVAKSRI TQMFTAKPQD WLVIANSAGY
GFTCQFENLL SRQKAGKSFI TLETGETLLK VTSYVPRETS LVACLAKSGK LHLFPLAEFK
QLTGGGKGVI TMALDDKDAL SAITISDGEV LKLSGTGRGG KAVELTLDAN DMAPYIGKRA
RKGKPINAGL KFPGF
//