PARC_BACSU
ID PARC_BACSU Reviewed; 806 AA.
AC Q45066; O30998;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 154.
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}; Synonyms=grlA;
GN OrderedLocusNames=BSU18100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969507; DOI=10.1099/13500872-142-11-3097;
RA Rose M., Entian K.-D.;
RT "New genes in the 170 degrees region of the Bacillus subtilis genome encode
RT DNA gyrase subunits, a thioredoxin, a xylanase and an amino acid
RT transporter.";
RL Microbiology 142:3097-3101(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / CB10;
RX PubMed=9539793; DOI=10.1073/pnas.95.8.4652;
RA Huang W.M., Libbey J.L., van de Hoeven P., Yu S.X.;
RT "Bipolar localization of Bacillus subtilis topoisomerase IV, an enzyme
RT required for chromosome segregation.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4652-4657(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 210.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
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 Cytoplasm. Note=Bipolarly localized.
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; Z73234; CAA97607.1; -; Genomic_DNA.
DR EMBL; AF024713; AAB81615.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13693.2; -; Genomic_DNA.
DR PIR; B69637; B69637.
DR RefSeq; NP_389692.2; NC_000964.3.
DR RefSeq; WP_003231550.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q45066; -.
DR SMR; Q45066; -.
DR STRING; 224308.BSU18100; -.
DR DrugCentral; Q45066; -.
DR PaxDb; Q45066; -.
DR PRIDE; Q45066; -.
DR EnsemblBacteria; CAB13693; CAB13693; BSU_18100.
DR GeneID; 937107; -.
DR KEGG; bsu:BSU18100; -.
DR PATRIC; fig|224308.179.peg.1972; -.
DR eggNOG; COG0188; Bacteria.
DR InParanoid; Q45066; -.
DR OMA; PRSNRID; -.
DR PhylomeDB; Q45066; -.
DR BioCyc; BSUB:BSU18100-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Cell membrane; Cytoplasm; DNA-binding; Isomerase; Membrane;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..806
FT /note="DNA topoisomerase 4 subunit A"
FT /id="PRO_0000145394"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 41
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 79
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 90
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 96
FT /note="Interaction with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT SITE 120
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00937"
FT CONFLICT 210
FT /note="V -> L (in Ref. 1; CAA97607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 91321 MW; 2CFC919CFC7D0BAF CRC64;
MSQPELFHDL PLEEVIGDRF GRYSKYIIQD RALPDARDGL KPVQRRILYA MHTDGNTFDK
NFRKAAKTVG NVIGNYHPHG DSSVYEAMVR MSQDWKVRNV LIEMHGNNGS IDGDPPAAMR
YTEARLSPIA SELLRDIDKN TVEFVPNFDD TSKEPVVLPA MFPNLLVNGS TGISAGYATD
IPPHHLGEVI DAVIKRIQMP SCSVDELMEV IKGPDFPTGG IIQGVDGIRK AYETGKGKII
IRGKAEIETI RGGREQIVIT EIPFEVNKAN LVKKMDEFRI DKKVEGISEV RDETDRTGLR
VVIELKKEAD AKGILNFLYK NTDLQITYNF NMVAIHNRRP MLMSLPSILD AYIGHQKEVV
TNRSVYELQK AKDRHHIVEG LMKALSILDE VIATIRSSSD KRDAKNNLIA KYEFTEPQAE
AIVSLQLYRL TNTDITALKE EAEELGKKIE ELESILSNDK KLLKVITNSL KALKKKYADT
RRSVIEEKIE EIKINLEVMV ASEDVYVTVT KDGYLKRTSQ RSFAASNGQD FGMKDTDRML
HQFEMNTTDV LLLFTNKGSY IYCPVHQLPD IRWKDMGQHF SNLITIDRDE TIVKAIPIKE
FDPSAYLLFF TKNGMVKKTE LTHYKAQRYS KALVALNLKG EDELIDVHVT NGESQIFMAT
HLGYGLWFGE DEVNVVGARA AGVKGINLKE DDFVVSGEIL QQSDSIVLFT QRGAVKRMSL
SEFEKTSRAK RGVVMLRELK KNPHRVVALF ACGLEQRLMA ETEKGDRKEL QTKELRTNDR
YSNGSFFFDE EESGKVTAVW RLHTEQ
