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GPR_CLOAB
ID   GPR_CLOAB               Reviewed;         327 AA.
AC   Q97JJ9;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Germination protease {ECO:0000255|HAMAP-Rule:MF_00626};
DE            EC=3.4.24.78 {ECO:0000255|HAMAP-Rule:MF_00626};
DE   AltName: Full=GPR endopeptidase {ECO:0000255|HAMAP-Rule:MF_00626};
DE   AltName: Full=Germination proteinase {ECO:0000255|HAMAP-Rule:MF_00626};
DE   AltName: Full=Spore protease {ECO:0000255|HAMAP-Rule:MF_00626};
DE   Flags: Precursor;
GN   Name=gpr {ECO:0000255|HAMAP-Rule:MF_00626}; OrderedLocusNames=CA_C1275;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Initiates the rapid degradation of small, acid-soluble
CC       proteins during spore germination. {ECO:0000255|HAMAP-Rule:MF_00626}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endopeptidase action with P4 Glu or Asp, P1 preferably Glu >
CC         Asp, P1' hydrophobic and P2' Ala.; EC=3.4.24.78;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00626};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00626}.
CC   -!- PTM: Autoproteolytically processed. The inactive tetrameric zymogen
CC       termed p46 autoprocesses to a smaller form termed p41, which is active
CC       only during spore germination. {ECO:0000255|HAMAP-Rule:MF_00626}.
CC   -!- SIMILARITY: Belongs to the peptidase A25 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00626}.
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DR   EMBL; AE001437; AAK79246.1; -; Genomic_DNA.
DR   PIR; C97057; C97057.
DR   RefSeq; NP_347906.1; NC_003030.1.
DR   RefSeq; WP_010964587.1; NC_003030.1.
DR   AlphaFoldDB; Q97JJ9; -.
DR   SMR; Q97JJ9; -.
DR   STRING; 272562.CA_C1275; -.
DR   MEROPS; A25.001; -.
DR   EnsemblBacteria; AAK79246; AAK79246; CA_C1275.
DR   GeneID; 44997781; -.
DR   KEGG; cac:CA_C1275; -.
DR   PATRIC; fig|272562.8.peg.1476; -.
DR   eggNOG; COG0680; Bacteria.
DR   HOGENOM; CLU_055087_1_0_9; -.
DR   OMA; PMGNYIT; -.
DR   OrthoDB; 799376at2; -.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009847; P:spore germination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1450; -; 1.
DR   HAMAP; MF_00626; Germination_prot; 1.
DR   InterPro; IPR023430; Pept_HybD-like_dom_sf.
DR   InterPro; IPR005080; Peptidase_A25.
DR   Pfam; PF03418; Peptidase_A25; 1.
DR   PIRSF; PIRSF019549; Peptidase_A25; 1.
DR   SUPFAM; SSF53163; SSF53163; 1.
DR   TIGRFAMs; TIGR01441; GPR; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Reference proteome; Zymogen.
FT   PROPEP          1..7
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00626"
FT                   /id="PRO_0000026872"
FT   CHAIN           8..327
FT                   /note="Germination protease"
FT                   /id="PRO_0000026873"
SQ   SEQUENCE   327 AA;  35651 MW;  8CD6C3D173296531 CRC64;
     MNSVRTDLAV EAREMYCEKT ENGDNGVRVD TKRIEDIEIT TVDVLNDKGE ERIRKQKGTY
     ITLDIPKVTL YDSEDIEEIS KVFADELSKI ISKAKLDSSM TVLVVGLGNW NITPDSLGPK
     VIGKLMVTRH LKKYIPDSID EGIRPVCAVA PGVLGITGME TGEIIRGIVQ NIKPDLIVCI
     DALAARKMGR VNSTIQIGNT GISPGSGVGN MRMELSQKTL GVPVIAVGVP TVVDAATMAN
     DTIDIVIEKM KGEVSEDSKF YSLLKAIDTE EKSQLIYEVL NPYVGDLLVT PKEVDMIMET
     LSKIIASGIN IALQPALELS EINKYVN
 
 
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