ID   CLPE_STRPN              Reviewed;         752 AA.
AC   P35594;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpE;
DE   AltName: Full=Exported protein 4;
GN   Name=clpE; Synonyms=exp4; OrderedLocusNames=SP_0820;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 600-692.
RC   STRAIN=R6x;
RX   PubMed=7934910; DOI=10.1111/j.1365-2958.1993.tb01233.x;
RA   Pearce B.J., Yin Y.B., Masure H.R.;
RT   "Genetic identification of exported proteins in Streptococcus pneumoniae.";
RL   Mol. Microbiol. 9:1037-1050(1993).
CC   -!- FUNCTION: Could be necessary for degrading proteins generated by
CC       certain types of stress. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By heat shock. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpE subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005672; AAK74952.1; -; Genomic_DNA.
DR   EMBL; L20558; AAA26880.1; -; Genomic_DNA.
DR   PIR; G95094; G95094.
DR   RefSeq; WP_000882523.1; NZ_AKVY01000001.1.
DR   AlphaFoldDB; P35594; -.
DR   SMR; P35594; -.
DR   STRING; 170187.SP_0820; -.
DR   PRIDE; P35594; -.
DR   EnsemblBacteria; AAK74952; AAK74952; SP_0820.
DR   KEGG; spn:SP_0820; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; ERMKAVM; -.
DR   PhylomeDB; P35594; -.
DR   BioCyc; SPNE170187:G1FZB-839-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Chaperone; Membrane; Metal-binding;
KW   Nucleotide-binding; Repeat; Stress response; Zinc; Zinc-finger.
FT   CHAIN           1..752
FT                   /note="ATP-dependent Clp protease ATP-binding subunit ClpE"
FT                   /id="PRO_0000191227"
FT   DOMAIN          365..400
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   ZN_FING         3..32
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   REGION          67..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..360
FT                   /note="I"
FT   REGION          413..604
FT                   /note="II"
FT   COMPBIAS        88..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         158..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         487..494
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   752 AA;  83814 MW;  376989EA320F0C88 CRC64;
     MLCQNCKIND STIHLYTNLN GKQKQIDLCQ NCYKIIKTDP NNSLFKGMTD LNNRDFDPFG
     DFFNDLNNFR PSSNTPPIPP TQSGGGYGGN GGYGSQNRGS AQTPPPSQEK GLLEEFGINV
     TEIARRGDID PVIGRDDEII RVIEILNRRT KNNPVLIGEP GVGKTAVVEG LAQKIVDGDV
     PHKLQGKQVI RLDVVSLVQG TGIRGQFEER MQKLMEEIRK REDIILFIDE IHEIVGAGSA
     SDGNMDAGNI LKPALARGEL QLVGATTLNE YRIIEKDAAL ERRMQPVKVD EPTVDETITI
     LKGIQKKYED YHHVQYTDAA IEAAATLSNR YIQDRFLPDK AIDLLDEAGS KMNLTLNFVD
     PKVIDQRLIE AENLKSQATR EEDFEKAAYF RDQIAKYKEM QKKKITDQDT PSISEKTIEH
     IIEQKTNIPV GDLKEKEQSQ LIHLAEDLKS HVIGQDDAVD KIAKAIRRNR VGLGTPNRPI
     GSFLFVGPTG VGKTELSKQL AIELFGSADS MIRFDMSEYM EKHSVAKLVG APPGYVGYDE
     AGQLTEKVRH NPYSLILLDE VEKAHPDVMH MFLQVLDDGR LTDGQGRTVS FKDAIIIMTS
     NAGTGKTEAS VGFGAAREGR TNSVLGELGN FFSPEFMNRF DGIIEFKALS KDNLLQIVEL
     MLADVNKRLS SNNIRLDVTD KVKEKLVDLG YDPKMGARPL RRTIQDYIED TITDYYLENP
     SEKDLKAVMT SKGNIQIKSA KKAEVKSSEK EK