(data stored in ACNUC7421 zone)

SWISSPROT: A4ATE2_MARSH

ID   A4ATE2_MARSH            Unreviewed;       182 AA.
AC   A4ATE2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=ATP-dependent Clp protease proteolytic subunit {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567};
DE            EC=3.4.21.92 {ECO:0000256|HAMAP-Rule:MF_00444};
DE   AltName: Full=Endopeptidase Clp {ECO:0000256|HAMAP-Rule:MF_00444};
GN   Name=clpP {ECO:0000256|HAMAP-Rule:MF_00444};
GN   OrderedLocusNames=FB2170_16546 {ECO:0000313|EMBL:EAR00712.1};
OS   Maribacter sp. (strain HTCC2170 / KCCM 42371).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=313603 {ECO:0000313|EMBL:EAR00712.1, ECO:0000313|Proteomes:UP000001602};
RN   [1] {ECO:0000313|EMBL:EAR00712.1, ECO:0000313|Proteomes:UP000001602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2170 / KCCM 42371 {ECO:0000313|Proteomes:UP000001602};
RX   PubMed=21037013; DOI=10.1128/JB.01207-10;
RA   Oh H.M., Kang I., Yang S.J., Jang Y., Vergin K.L., Giovannoni S.J.,
RA   Cho J.C.;
RT   "Complete genome sequence of strain HTCC2170, a novel member of the
RT   genus Maribacter in the family Flavobacteriaceae.";
RL   J. Bacteriol. 193:303-304(2011).
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:0000256|HAMAP-Rule:MF_00444}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins to small peptides in the presence
CC         of ATP and magnesium. Alpha-casein is the usual test substrate.
CC         In the absence of ATP, only oligopeptides shorter than five
CC         residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and
CC         Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and
CC         -Tyr-|-Trp bonds also occurs).; EC=3.4.21.92;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|PROSITE-
CC         ProRule:PRU10086};
CC   -!- SUBUNIT: Fourteen ClpP subunits assemble into 2 heptameric rings
CC       which stack back to back to give a disk-like structure with a
CC       central cavity, resembling the structure of eukaryotic
CC       proteasomes. {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444}.
CC   -!- SIMILARITY: Belongs to the peptidase S14 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00444, ECO:0000256|RuleBase:RU003567}.
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DR   EMBL; CP002157; EAR00712.1; -; Genomic_DNA.
DR   RefSeq; WP_013304515.1; NC_014472.1.
DR   STRING; 313603.FB2170_16546; -.
DR   MEROPS; S14.005; -.
DR   EnsemblBacteria; EAR00712; EAR00712; FB2170_16546.
DR   KEGG; fbc:FB2170_16546; -.
DR   eggNOG; ENOG4108N9J; Bacteria.
DR   eggNOG; COG0740; LUCA.
DR   HOGENOM; HOG000285833; -.
DR   KO; K01358; -.
DR   OMA; ERKVFLW; -.
DR   OrthoDB; 1728970at2; -.
DR   BioCyc; MSP313603:G1GNS-87-MONOMER; -.
DR   Proteomes; UP000001602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR10381; PTHR10381; 1.
DR   Pfam; PF00574; CLP_protease; 1.
DR   PRINTS; PR00127; CLPPROTEASEP.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00382; CLP_PROTEASE_HIS; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4ATE2.
DR   SWISS-2DPAGE; A4ATE2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001602};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00444};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00444};
KW   Protease {ECO:0000256|HAMAP-Rule:MF_00444,
KW   ECO:0000313|EMBL:EAR00712.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001602};
KW   Serine protease {ECO:0000256|HAMAP-Rule:MF_00444}.
FT   ACT_SITE     89     89       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_00444}.
FT   ACT_SITE    114    114       {ECO:0000256|HAMAP-Rule:MF_00444,
FT                                ECO:0000256|PROSITE-ProRule:PRU10086}.
SQ   SEQUENCE   182 AA;  20266 MW;  0D84BE5BB252B2C1 CRC64;
     MSSKKGKVQE AIDEKLLEER KVFLWGMVDD DSAKHVIDRL LYLDMQNNKE IQLFINSPGG
     YVTSGFAMYD TIKSLKSPVS TICTGLAASM GSILLSVGKK GRRFIQPHAQ VMIHQPSGGA
     RGQASNIEIQ AKEIIKTKEL SAQILADNCG QDFDTVMRDF DRDYWMNAEE SIEYGIVDGV
     LE
//

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