RACA_BACSU
ID RACA_BACSU Reviewed; 184 AA.
AC P45870;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Chromosome-anchoring protein RacA;
GN Name=racA; Synonyms=ywkC; OrderedLocusNames=BSU37030;
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=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(1997).
RN [2]
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=12493822; DOI=10.1126/science.1079914;
RA Ben-Yehuda S., Rudner D.Z., Losick R.;
RT "RacA, a bacterial protein that anchors chromosomes to the cell poles.";
RL Science 299:532-536(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH DIVIVA PROTEIN.
RC STRAIN=168;
RX PubMed=12950914; DOI=10.1046/j.1365-2958.2003.03643.x;
RA Wu L.J., Errington J.;
RT "RacA and the Soj-Spo0J system combine to effect polar chromosome
RT segregation in sporulating Bacillus subtilis.";
RL Mol. Microbiol. 49:1463-1475(2003).
RN [5]
RP DNA-BINDING.
RC STRAIN=168 / PY79;
RX PubMed=15780934; DOI=10.1016/j.molcel.2005.02.023;
RA Ben-Yehuda S., Fujita M., Liu X.S., Gorbatyuk B., Skoko D., Yan J.,
RA Marko J.F., Liu J.S., Eichenberger P., Rudner D.Z., Losick R.;
RT "Defining a centromere-like element in Bacillus subtilis by identifying the
RT binding sites for the chromosome-anchoring protein RacA.";
RL Mol. Cell 17:773-782(2005).
CC -!- FUNCTION: Required for the formation of axial filaments and for
CC anchoring the origin regions at the cell poles in sporulating cells,
CC thus ensuring proper chromosome segregation in the prespore. Binds in a
CC dispersed manner throughout the chromosome but preferentially to sites
CC clustered in the origin portion of the chromosome, causing condensation
CC of the chromosome and its remodeling into an elongated, anchored
CC structure. {ECO:0000269|PubMed:12493822, ECO:0000269|PubMed:12950914}.
CC -!- INTERACTION:
CC P45870; P37475: spoIIE; NbExp=3; IntAct=EBI-5242400, EBI-9304781;
CC P45870; P37562: yabT; NbExp=3; IntAct=EBI-5242400, EBI-9303331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12493822}.
CC Note=Localizes to cell poles and nucleoid, in a DivIVA-dependent
CC manner.
CC -!- DEVELOPMENTAL STAGE: Expressed at the early stages of sporulation.
CC -!- SIMILARITY: Belongs to the RacA family. {ECO:0000305}.
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DR EMBL; Z49782; CAA89882.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15720.1; -; Genomic_DNA.
DR PIR; S55435; S55435.
DR RefSeq; NP_391584.1; NC_000964.3.
DR RefSeq; WP_003227642.1; NZ_JNCM01000034.1.
DR PDB; 5I41; X-ray; 1.80 A; B=1-66.
DR PDB; 5I44; X-ray; 2.62 A; A/B/D/E/F/G/H/I/J/K=1-66.
DR PDBsum; 5I41; -.
DR PDBsum; 5I44; -.
DR AlphaFoldDB; P45870; -.
DR SMR; P45870; -.
DR IntAct; P45870; 33.
DR STRING; 224308.BSU37030; -.
DR PaxDb; P45870; -.
DR PRIDE; P45870; -.
DR EnsemblBacteria; CAB15720; CAB15720; BSU_37030.
DR GeneID; 937043; -.
DR KEGG; bsu:BSU37030; -.
DR PATRIC; fig|224308.179.peg.4010; -.
DR eggNOG; COG0789; Bacteria.
DR OMA; WVKQLNL; -.
DR BioCyc; BSUB:BSU37030-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008356; P:asymmetric cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-UniRule.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01170; RacA; 1.
DR InterPro; IPR023522; Chrosome_anchoring_RacA.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR Pfam; PF13411; MerR_1; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome partition; Coiled coil;
KW Cytoplasm; DNA-binding; Reference proteome; Sporulation.
FT CHAIN 1..184
FT /note="Chromosome-anchoring protein RacA"
FT /id="PRO_0000049979"
FT DNA_BIND 3..23
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT COILED 75..156
FT /evidence="ECO:0000255"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:5I41"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:5I41"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5I41"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:5I41"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5I41"
SQ SEQUENCE 184 AA; 21070 MW; 1695B10FDFE10F22 CRC64;
MNTNMVASEL GVSAKTVQRW VKQLNLPAER NELGHYSFTA EDVKVLKSVQ KQISEGTAIQ
DIHLPKSAKK RTGFLVQKTS SDTERRIEQL EQKLDTLLQQ RQDESELMAR MSELERQLKQ
KADEGVSYQL LQHRREIDDI LADLQSLTSQ MKEFTAHSIP ETAAASEKTK TRKKPLLSLF
KFQT
