ID   PARC_NEIGO              Reviewed;         768 AA.
AC   P48374;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
DE            EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00936};
DE   AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00936};
GN   Name=parC {ECO:0000255|HAMAP-Rule:MF_00936};
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RX   PubMed=7830580; DOI=10.1111/j.1365-2958.1994.tb01297.x;
RA   Belland R.J., Morrison S.G., Ison C., Huang W.M.;
RT   "Neisseria gonorrhoeae acquires mutations in analogous regions of gyrA and
RT   parC in fluoroquinolone-resistant isolates.";
RL   Mol. Microbiol. 14:371-380(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MS11;
RA   Belland R.J.;
RL   Submitted (APR-1994) 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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00936};
CC   -!- SUBUNIT: Heterotetramer composed of ParC and ParE.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00936};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00936}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. ParC type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00936}.
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DR   EMBL; U08907; AAA82151.1; -; Genomic_DNA.
DR   PIR; S60780; S60780.
DR   AlphaFoldDB; P48374; -.
DR   SMR; P48374; -.
DR   ChEMBL; CHEMBL2363077; -.
DR   DrugCentral; P48374; -.
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; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 1.
DR   HAMAP; MF_00936; ParC_type1; 1.
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   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   Cell membrane; DNA-binding; Isomerase; Membrane; Topoisomerase.
FT   CHAIN           1..768
FT                   /note="DNA topoisomerase 4 subunit A"
FT                   /id="PRO_0000145403"
FT   ACT_SITE        126
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            46
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            82
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            84
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
FT   SITE            125
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00936"
SQ   SEQUENCE   768 AA;  84896 MW;  DAD11ECAC172F6EE CRC64;
     MNTQPHASHT DSNTLMLGRY AERAYLEYAM SVVKGRALPE VSDGQKPVQR RILFAMRDMG
     LTAGAKPVKS ARVVGEILGK YHPHGDSSAY EAMVRMAQDF TLRYPLIDGI GNFGSRDGDG
     AAAMRYTEAR LTPIAELLLS EINQGTVDFM PNYDGAFDEP LHLPARLPMV LLNGASGIAV
     GMATEIPSHN LNEVTQAAIA LLKKPTLETA DLMQYIPAPD FAGGGQIITP ADELRRIYET
     GKGSVRVRAR YEIEKLARGQ WRVIVTELPP NANSAKILAE IEEQTNPKPK AGKKQLNQDR
     LNTKKLMLDL IDRVRDESDG EHPVRLVFEP KSSRIDTDTF INTLMAQTSL EGNVSMNLVM
     MGLDNRPAQK NLKTILQEWL DFRIVTVTRR LKFRLNQVEK RLHILEGRLK VFLHIDEVIK
     VIRESDDPKA DLMAVFGLTE IQAEDILEIR LRQLARLEGF KLEKELNELR EEQGRLNIFL
     GDENEKRKLI IKEMQADMKQ FGDARRTLVE EAGRAVLTQT AADEPITLIL SEKGWIRSRA
     GHNLDLSQTA FKEGDRLKQT LEGPHCFTRR HPRFIRGRTY SIDAAEIPGG RGDGVPVSSL
     IELQNGAKPV AMLTGLPEQH YLLSSSGGYG FIAKLGDMVG RVKAGKVVMT ADSGETVLPP
     VAVYASSFIN PDCKIIAATS QNRALAFPIG ELKIMAKGKG LQIIGLNAGE SMTHTAVSSE
     PEILIESEGR RGAAHKDRLP VALIEAKRGK KGRLLPISGS LKQLSSPK