CLPP_NEIMB
ID CLPP_NEIMB Reviewed; 204 AA.
AC Q9JZ38;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000255|HAMAP-Rule:MF_00444};
DE EC=3.4.21.92 {ECO:0000255|HAMAP-Rule:MF_00444};
DE AltName: Full=Endopeptidase Clp {ECO:0000255|HAMAP-Rule:MF_00444};
GN Name=clpP {ECO:0000255|HAMAP-Rule:MF_00444}; OrderedLocusNames=NMB1312;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: Cleaves peptides in various proteins in a process that
CC requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a
CC major role in the degradation of misfolded proteins.
CC {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins to small peptides in the presence of
CC ATP and magnesium. alpha-casein is the usual test substrate. In the
CC absence of ATP, only oligopeptides shorter than five residues are
CC hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-
CC Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also
CC occurs).; EC=3.4.21.92; Evidence={ECO:0000255|HAMAP-Rule:MF_00444};
CC -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings which
CC stack back to back to give a disk-like structure with a central cavity,
CC resembling the structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
CC -!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000255|HAMAP-
CC Rule:MF_00444}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF41687.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE002098; AAF41687.1; ALT_INIT; Genomic_DNA.
DR PIR; F81098; F81098.
DR RefSeq; NP_274331.1; NC_003112.2.
DR RefSeq; WP_002225167.1; NC_003112.2.
DR PDB; 5DKP; X-ray; 2.38 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/a/b/c/d/e/f/g/h/i/j/k/l/m/n=1-204.
DR PDB; 6NAH; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-204.
DR PDB; 6NAQ; X-ray; 2.02 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-204.
DR PDB; 6NAW; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-204.
DR PDB; 6NAY; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b=1-204.
DR PDB; 6VFS; EM; 3.30 A; H/I/J/K/L/M/N/O/P/Q/R/S/T/U=1-204.
DR PDB; 6VFX; EM; 2.90 A; H/I/J/K/L/M/N/O/P/Q/R/S/T/U=1-204.
DR PDB; 6W9T; X-ray; 1.64 A; A/B/C/D/E/F/G=6-204.
DR PDBsum; 5DKP; -.
DR PDBsum; 6NAH; -.
DR PDBsum; 6NAQ; -.
DR PDBsum; 6NAW; -.
DR PDBsum; 6NAY; -.
DR PDBsum; 6VFS; -.
DR PDBsum; 6VFX; -.
DR PDBsum; 6W9T; -.
DR AlphaFoldDB; Q9JZ38; -.
DR SMR; Q9JZ38; -.
DR STRING; 122586.NMB1312; -.
DR MEROPS; S14.001; -.
DR PaxDb; Q9JZ38; -.
DR EnsemblBacteria; AAF41687; AAF41687; NMB1312.
DR KEGG; nme:NMB1312; -.
DR PATRIC; fig|122586.8.peg.1646; -.
DR HOGENOM; CLU_058707_3_2_4; -.
DR OMA; RDYWMKA; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009368; C:endopeptidase Clp complex; IBA:GO_Central.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IBA:GO_Central.
DR CDD; cd07017; S14_ClpP_2; 1.
DR HAMAP; MF_00444; ClpP; 1.
DR InterPro; IPR001907; ClpP.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR023562; ClpP/TepA.
DR InterPro; IPR033135; ClpP_His_AS.
DR InterPro; IPR018215; ClpP_Ser_AS.
DR PANTHER; PTHR10381; PTHR10381; 1.
DR Pfam; PF00574; CLP_protease; 1.
DR PRINTS; PR00127; CLPPROTEASEP.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00493; clpP; 1.
DR PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
DR PROSITE; PS00381; CLP_PROTEASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..204
FT /note="ATP-dependent Clp protease proteolytic subunit"
FT /id="PRO_0000179602"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT ACT_SITE 127
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00444"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:5DKP"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:5DKP"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:6W9T"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:6W9T"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5DKP"
FT STRAND 64..70
FT /evidence="ECO:0007829|PDB:6W9T"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:6W9T"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:6NAQ"
FT HELIX 139..164
FT /evidence="ECO:0007829|PDB:6W9T"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6NAH"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:6W9T"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6W9T"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6NAY"
SQ SEQUENCE 204 AA; 22704 MW; C99673795060F9C8 CRC64;
MSFDNYLVPT VIEQSGRGER AFDIYSRLLK ERIVFLVGPV TDESANLVVA QLLFLESENP
DKDIFFYINS PGGSVTAGMS IYDTMNFIKP DVSTLCLGQA ASMGAFLLSA GEKGKRFALP
NSRIMIHQPL ISGGLGGQAS DIEIHARELL KIKEKLNRLM AKHCDRDLAD LERDTDRDNF
MSAEEAKEYG LIDQILENRA SLRL
