(data stored in ACNUC7421 zone)

SWISSPROT: CLPC_BACSU

ID   CLPC_BACSU              Reviewed;         810 AA.
AC   P37571;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 143.
DE   RecName: Full=Negative regulator of genetic competence ClpC/MecB;
GN   Name=clpC; Synonyms=mecB; OrderedLocusNames=BSU00860;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8016066; DOI=10.1073/pnas.91.13.5788;
RA   Msadek T., Kunst F., Rapoport G.;
RT   "MecB of Bacillus subtilis, a member of the ClpC ATPase family, is a
RT   pleiotropic regulator controlling competence gene expression and growth at
RT   high temperature.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5788-5792(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 211-387.
RX   PubMed=8195092; DOI=10.1128/jb.176.11.3360-3367.1994;
RA   Krueger E., Voelker U., Hecker M.;
RT   "Stress induction of clpC in Bacillus subtilis and its involvement in
RT   stress tolerance.";
RL   J. Bacteriol. 176:3360-3367(1994).
CC   -!- FUNCTION: Competence gene repressor; required for cell growth at high
CC       temperature. Negative regulator of comK expression. May interact with
CC       MecA to negatively regulate comK.
CC   -!- INTERACTION:
CC       P37958:mecA; NbExp=11; IntAct=EBI-7349302, EBI-5254676;
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC       {ECO:0000305}.
DR   EMBL; U02604; AAA19233.1; -; Genomic_DNA.
DR   EMBL; D26185; BAA05320.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11862.1; -; Genomic_DNA.
DR   EMBL; X75930; CAA53534.1; -; Genomic_DNA.
DR   PIR; I40508; I40508.
DR   RefSeq; NP_387967.1; NC_000964.3.
DR   RefSeq; WP_003235011.1; NZ_JNCM01000029.1.
DR   PDB; 2K77; NMR; -; A=1-145.
DR   PDB; 2Y1Q; X-ray; 1.50 A; A=1-150.
DR   PDB; 2Y1R; X-ray; 2.60 A; A/B/C/D/E/F/G/H=1-149.
DR   PDB; 3J3R; EM; 9.40 A; A/B/C/D/E/F=1-810.
DR   PDB; 3J3S; EM; 11.00 A; A/B/C/D/E/F=1-810.
DR   PDB; 3J3T; EM; 9.00 A; A/B/C/D/E/F=1-810.
DR   PDB; 3J3U; EM; 10.00 A; A/B/C/D/E/F=1-810.
DR   PDB; 3PXG; X-ray; 3.65 A; A/B/C/D/E/F=1-485.
DR   PDB; 3PXI; X-ray; 6.93 A; A/B/C=1-810.
DR   PDB; 5HBN; X-ray; 1.60 A; A=1-150.
DR   PDBsum; 2K77; -.
DR   PDBsum; 2Y1Q; -.
DR   PDBsum; 2Y1R; -.
DR   PDBsum; 3J3R; -.
DR   PDBsum; 3J3S; -.
DR   PDBsum; 3J3T; -.
DR   PDBsum; 3J3U; -.
DR   PDBsum; 3PXG; -.
DR   PDBsum; 3PXI; -.
DR   PDBsum; 5HBN; -.
DR   SMR; P37571; -.
DR   DIP; DIP-43708N; -.
DR   IntAct; P37571; 5.
DR   MINT; P37571; -.
DR   STRING; 224308.BSU00860; -.
DR   jPOST; P37571; -.
DR   PaxDb; P37571; -.
DR   PRIDE; P37571; -.
DR   DNASU; 938481; -.
DR   EnsemblBacteria; CAB11862; CAB11862; BSU00860.
DR   GeneID; 938481; -.
DR   KEGG; bsu:BSU00860; -.
DR   PATRIC; fig|224308.179.peg.87; -.
DR   eggNOG; COG0542; LUCA.
DR   HOGENOM; HOG000218210; -.
DR   InParanoid; P37571; -.
DR   KO; K03696; -.
DR   OMA; QDPKRPI; -.
DR   PhylomeDB; P37571; -.
DR   BioCyc; BSUB:BSU00860-MONOMER; -.
DR   EvolutionaryTrace; P37571; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004176; Clp_N.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37571.
DR   SWISS-2DPAGE; P37571.
KW   3D-structure; ATP-binding; Chaperone; Competence; Nucleotide-binding;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..810
FT                   /note="Negative regulator of genetic competence ClpC/MecB"
FT                   /id="PRO_0000191228"
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          417..452
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   NP_BIND         208..215
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   NP_BIND         545..552
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          80..144
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          163..410
FT                   /note="I"
FT   REGION          471..662
FT                   /note="II"
FT   HELIX           8..23
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   STRAND          27..29
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           31..41
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           45..52
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           57..68
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           82..97
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   STRAND          101..103
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           105..115
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           119..126
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
FT   HELIX           131..143
FT                   /evidence="ECO:0000244|PDB:2Y1Q"
SQ   SEQUENCE   810 AA;  90119 MW;  9592231886C2E870 CRC64;
     MMFGRFTERA QKVLALAQEE ALRLGHNNIG TEHILLGLVR EGEGIAAKAL QALGLGSEKI
     QKEVESLIGR GQEMSQTIHY TPRAKKVIEL SMDEARKLGH SYVGTEHILL GLIREGEGVA
     ARVLNNLGVS LNKARQQVLQ LLGSNETGSS AAGTNSNANT PTLDSLARDL TAIAKEDSLD
     PVIGRSKEIQ RVIEVLSRRT KNNPVLIGEP GVGKTAIAEG LAQQIINNEV PEILRDKRVM
     TLDMGTVVAG TKYRGEFEDR LKKVMDEIRQ AGNIILFIDE LHTLIGAGGA EGAIDASNIL
     KPSLARGELQ CIGATTLDEY RKYIEKDAAL ERRFQPIQVD QPSVDESIQI LQGLRDRYEA
     HHRVSITDDA IEAAVKLSDR YISDRFLPDK AIDLIDEAGS KVRLRSFTTP PNLKELEQKL
     DEVRKEKDAA VQSQEFEKAA SLRDTEQRLR EQVEDTKKSW KEKQGQENSE VTVDDIAMVV
     SSWTGVPVSK IAQTETDKLL NMENILHSRV IGQDEAVVAV AKAVRRARAG LKDPKRPIGS
     FIFLGPTGVG KTELARALAE SIFGDEESMI RIDMSEYMEK HSTSRLVGSP PGYVGYDEGG
     QLTEKVRRKP YSVVLLDEIE KAHPDVFNIL LQVLEDGRLT DSKGRTVDFR NTILIMTSNV
     GASELKRNKY VGFNVQDETQ NHKDMKDKVM GELKRAFRPE FINRIDEIIV FHSLEKKHLT
     EIVSLMSDQL TKRLKEQDLS IELTDAAKAK VAEEGVDLEY GARPLRRAIQ KHVEDRLSEE
     LLRGNIHKGQ HIVLDVEDGE FVVKTTAKTN
//

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