PARC_STAAS
ID PARC_STAAS Reviewed; 800 AA.
AC Q6G9K4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=DNA topoisomerase 4 subunit A {ECO:0000255|HAMAP-Rule:MF_00937};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_00937};
DE AltName: Full=Topoisomerase IV subunit A {ECO:0000255|HAMAP-Rule:MF_00937};
GN Name=parC {ECO:0000255|HAMAP-Rule:MF_00937}; OrderedLocusNames=SAS1295;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-491.
RA Carr S.B., Makris G., Thomas C.D., Phillips S.E.V.;
RT "Crystal structure of a 59 kDa fragment of topoisomerase IV subunit A
RT (GrlA) from Staphylococcus aureus.";
RL Submitted (JUL-2011) to the PDB data bank.
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_00937}.
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_00937};
CC -!- SUBUNIT: Heterotetramer composed of ParC and ParE. {ECO:0000255|HAMAP-
CC Rule:MF_00937}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00937};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00937}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. ParC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_00937}.
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DR EMBL; BX571857; CAG43072.1; -; Genomic_DNA.
DR RefSeq; WP_001289571.1; NC_002953.3.
DR PDB; 2INR; X-ray; 2.80 A; A=2-491.
DR PDBsum; 2INR; -.
DR AlphaFoldDB; Q6G9K4; -.
DR SMR; Q6G9K4; -.
DR KEGG; sas:SAS1295; -.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OMA; PRSNRID; -.
DR BRENDA; 5.6.2.2; 3352.
DR EvolutionaryTrace; Q6G9K4; -.
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_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 PANTHER; PTHR43493:SF9; PTHR43493:SF9; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 5.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
DR TIGRFAMs; TIGR01061; parC_Gpos; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; DNA-binding; Isomerase; Membrane;
KW Topoisomerase.
FT CHAIN 1..800
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145413"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 39
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 75
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 77
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 88
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 94
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 118
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:2INR"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2INR"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2INR"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 162..166
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:2INR"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 223..232
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 311..316
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 343..384
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 432..455
FT /evidence="ECO:0007829|PDB:2INR"
FT HELIX 457..475
FT /evidence="ECO:0007829|PDB:2INR"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:2INR"
SQ SEQUENCE 800 AA; 90966 MW; EBE92B475F18EB5C CRC64;
MSEIIQDLSL EDVLGDRFGR YSKYIIQERA LPDVRDGLKP VQRRILYAMY SSGNTHDKNF
RKSAKTVGDV IGQYHPHGDS SVYEAMVRLS QDWKLRHVLI EMHGNNGSID NDPPAAMRYT
EAKLSLLAEE LLRDINKETV SFIPNYDDTT LEPMVLPSRF PNLLVNGSTG ISAGYATDIP
PHNLAEVIQA TLKYIDNPDI TVNQLMKYIK GPDFPTGGII QGIDGIKKAY ESGKGRIIVR
SKVEEETLRN GRKQLIITEI PYEVNKSSLV KRIDELRADK KVDGIVEVRD ETDRTGLRIA
IELKKDVNSE SIKNYLYKNS DLQISYNFNM VAISDGRPKL MGIRQIIDSY LNHQIEVVAN
RTKFELDNAE KRMHIVEGLI KALSILDKVI ELIRSSKNKR DAKENLIEVY EFTEEQAEAI
VMLQLYRLTN TDIVALEGEH KELEALIKQL RHILDNHDAL LNVIKEELNE IKKKFKSERL
SLIEAEIEEI KIDKEVMVPS EEVILSMTRH GYIKRTSIRS FNASGVEDIG LKDGDSLLKH
QEVNTQDTVL VFTNKGRYLF IPVHKLADIR WKELGQHVSQ IVPIEEDEVV INVFNEKDFN
TDAFYVFATQ NGMIKKSTVP LFKTTRFNKP LIATKVKEND DLISVMRFEK DQLITVITNK
GMSLTYNTSE LSDTGLRAAG VKSINLKAED FVVVTEGVSE NDTILMATQR GSLKRISFKI
LQVAKRAQRG ITLLKELKKN PHRIVAAHVV TGEHSQYTLY SKSNEEHGLI NDIHKSEQYT
NGSFIVDTDD FGEVIDMYIS
