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Entry: A0A1I4ZEQ9_9NEIS
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Original site: A0A1I4ZEQ9_9NEIS 
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
//
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