GSEP_BACLD
ID GSEP_BACLD Reviewed; 316 AA.
AC P80057; Q65NR6;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Glutamyl endopeptidase;
DE EC=3.4.21.19;
DE AltName: Full=Glutamate-specific endopeptidase;
DE Short=GSE;
DE Flags: Precursor;
GN Name=blaSE; Synonyms=mpr; OrderedLocusNames=BLi00340, BL01804;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1429718; DOI=10.1016/s0021-9258(18)35906-4;
RA Kakudo S., Kikuchi N., Kitadokoro K., Fujiwara T., Nakamura E., Okamoto H.,
RA Shin M., Tamaki M., Teraoka H., Tsuzuki H., Yoshida N.;
RT "Purification, characterization, cloning, and expression of a glutamic
RT acid-specific protease from Bacillus licheniformis ATCC 14580.";
RL J. Biol. Chem. 267:23782-23788(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
RN [4]
RP PROTEIN SEQUENCE OF 95-316.
RX PubMed=1346764; DOI=10.1111/j.1432-1033.1992.tb16619.x;
RA Svendsen I., Breddam K.;
RT "Isolation and amino acid sequence of a glutamic acid specific
RT endopeptidase from Bacillus licheniformis.";
RL Eur. J. Biochem. 204:165-171(1992).
CC -!- FUNCTION: Specific for hydrolysis of peptide bonds on the carboxyl side
CC of acidic amino acid residues, with a strong preference for Glu.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.; EC=3.4.21.19;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10083};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
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DR EMBL; D10060; BAA00949.1; -; Genomic_DNA.
DR EMBL; AE017333; AAU39298.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU21945.1; -; Genomic_DNA.
DR PIR; A45134; A45134.
DR AlphaFoldDB; P80057; -.
DR SMR; P80057; -.
DR STRING; 279010.BL01804; -.
DR MEROPS; S01.271; -.
DR EnsemblBacteria; AAU21945; AAU21945; BL01804.
DR KEGG; bld:BLi00340; -.
DR KEGG; bli:BL01804; -.
DR eggNOG; COG3591; Bacteria.
DR HOGENOM; CLU_073589_0_2_9; -.
DR OMA; DTYGCQS; -.
DR Proteomes; UP000000606; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR008256; Peptidase_S1B.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR028301; V8_his_AS.
DR InterPro; IPR000126; V8_ser_AS.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00839; V8PROTEASE.
DR SUPFAM; SSF50494; SSF50494; 1.
DR PROSITE; PS00672; V8_HIS; 1.
DR PROSITE; PS00673; V8_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT PROPEP 31..94
FT /evidence="ECO:0000269|PubMed:1346764"
FT /id="PRO_0000026900"
FT CHAIN 95..316
FT /note="Glutamyl endopeptidase"
FT /id="PRO_0000026901"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT ACT_SITE 261
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT DISULFID 126..142
FT DISULFID 275..279
SQ SEQUENCE 316 AA; 33611 MW; 96D7552CB7089B09 CRC64;
MVSKKSVKRG LITGLIGISI YSLGMHPAQA APSPHTPVSS DPSYKAETSV TYDPNIKSDQ
YGLYSKAFTG TGKVNETKEK AEKKSPAKAP YSIKSVIGSD DRTRVTNTTA YPYRAIVHIS
SSIGSCTGWM IGPKTVATAG HCIYDTSSGS FAGTATVSPG RNGTSYPYGS VKSTRYFIPS
GWRSGNTNYD YGAIELSEPI GNTVGYFGYS YTTSSLVGTT VTISGYPGDK TAGTQWQHSG
PIAISETYKL QYAMDTYGGQ SGSPVFEQSS SRTNCSGPCS LAVHTNGVYG GSSYNRGTRI
TKEVFDNLTN WKNSAQ
