CLPE_BACSU
ID CLPE_BACSU Reviewed; 699 AA.
AC O31673;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE;
DE AltName: Full=ATPase ClpE;
DE AltName: Full=Heat shock protein HSP1;
GN Name=clpE; OrderedLocusNames=BSU13700;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP INDUCTION BY HEAT SHOCK.
RX PubMed=10320580; DOI=10.1046/j.1365-2958.1999.01374.x;
RA Derre I., Rapoport G., Devine K., Rose M., Msadek T.;
RT "ClpE, a novel type of HSP100 ATPase, is part of the CtsR heat shock
RT regulon of Bacillus subtilis.";
RL Mol. Microbiol. 32:581-593(1999).
RN [3]
RP INTERACTION WITH CLPP, INDUCTION, AND PTM.
RX PubMed=14679237; DOI=10.1128/jb.186.1.179-191.2004;
RA Gerth U., Kirstein J., Mostertz J., Waldminghaus T., Miethke M., Kock H.,
RA Hecker M.;
RT "Fine-tuning in regulation of Clp protein content in Bacillus subtilis.";
RL J. Bacteriol. 186:179-191(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, ZINC-FINGER, AND MUTAGENESIS OF
RP 29-CYS--CYS-32.
RC STRAIN=168;
RX PubMed=16788169; DOI=10.1128/jb.00287-06;
RA Miethke M., Hecker M., Gerth U.;
RT "Involvement of Bacillus subtilis ClpE in CtsR degradation and protein
RT quality control.";
RL J. Bacteriol. 188:4610-4619(2006).
CC -!- FUNCTION: ATPase essential both for efficient CtsR-dependent gene
CC derepression during heat stress and for rerepression. Together with
CC ClpP, degrades the global regulator CtsR after heat shock. Is also
CC involved in disaggregation of heat-denatured proteins. Has thus a role
CC in overall protein quality control in response to heat stress.
CC {ECO:0000269|PubMed:16788169}.
CC -!- SUBUNIT: Interacts with ClpP. {ECO:0000269|PubMed:14679237}.
CC -!- INDUCTION: By heat shock via the relief of repression carried out by
CC the transcriptional regulator CtsR. {ECO:0000269|PubMed:10320580,
CC ECO:0000269|PubMed:14679237}.
CC -!- PTM: ClpE is a very short-lived protein, that is, at least in the
CC soluble cell fraction, degraded mainly by ClpCP.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a retardation of
CC CtsR-dependent gene induction as well as a delayed restoration of the
CC repressed stage. They also show a significant delay in disaggregation
CC of heat-generated insoluble protein aggregates.
CC {ECO:0000269|PubMed:16788169}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpE subfamily.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13243.1; -; Genomic_DNA.
DR PIR; A69601; A69601.
DR RefSeq; NP_389253.1; NC_000964.3.
DR RefSeq; WP_009967104.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31673; -.
DR SMR; O31673; -.
DR STRING; 224308.BSU13700; -.
DR jPOST; O31673; -.
DR PaxDb; O31673; -.
DR PRIDE; O31673; -.
DR EnsemblBacteria; CAB13243; CAB13243; BSU_13700.
DR GeneID; 939289; -.
DR KEGG; bsu:BSU13700; -.
DR PATRIC; fig|224308.179.peg.1487; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; O31673; -.
DR OMA; SFNRKKE; -.
DR PhylomeDB; O31673; -.
DR BioCyc; BSUB:BSU13700-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
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; 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 PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
DR PROSITE; PS50151; UVR; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding;
KW Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..699
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpE"
FT /id="PRO_0000390779"
FT DOMAIN 325..360
FT /note="UVR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT ZN_FING 3..32
FT /note="C4-type"
FT BINDING 119..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 446..453
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 29..32
FT /note="CETC->SETS: 10% of wild-type ATPase activity."
FT /evidence="ECO:0000269|PubMed:16788169"
SQ SEQUENCE 699 AA; 77906 MW; 5F45A749CF42A0AA CRC64;
MRCQHCHQNE ATIRLNMQIN SVHKQMVLCE TCYNELTRKP SMSMGPQSFG FPFEQAFQPK
EQSAAKQSEK KGLLDELAQN ITNGAKAGLI DPVIGRDDEV ARVIEILNRR NKNNPVLIGE
PGVGKTAIAE GLALKIAEGD VPNKLKNKEL YLLDVASLVA NTGIRGQFEE RMKQLITELK
ERKNVILFID EIHLLVGAGS AEGSMDAGNI LKPALARGEL QVIGATTLKE YRQIEKDAAL
ERRFQPVMVQ EPSIEQAILI LQGIKDKYEA YHGVTFSDEA IKACVTLSSR YIQDRHLPDK
AIDLLDEAGS KANLLIDELN DEDAAERLTA IEAEKTKALE EENYELAAKL RDEELALEKK
LNSSSAHTAV TVEAEHIQEI VEQKTGIPVG KLQADEQTKM KELEAKLHER VIGQEAAVQK
VAKAVRRSRA GLKSKNRPVG SFLFVGPTGV GKTELSKTLA DELFGTKDAI IRLDMSEYME
KHAVSKIIGS PPGYVGHEEA GQLTEKVRRN PYSIVLLDEI EKAHPDVQHM FLQIMEDGRL
TDSQGRTVSF KDTVIIMTSN AGAGEKQTKV GFQSDDSVIE EQTLIDSLSM FFKPEFLNRF
DSIIEFRSLE KEHLVKIVSL LLGELEETLA ERGISLNVTD EAKEKIAELG YHPSFGARPL
RRTIQEWVED EMTDLLLDNG EITSFHVILE DDKIKVRAK
