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Database: UniProt/SWISS-PROT
Entry: NPRM_BACMD
LinkDB: NPRM_BACMD
Original site: NPRM_BACMD 
ID   NPRM_BACMD              Reviewed;         562 AA.
AC   D5DEH5; Q00891;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   05-DEC-2018, entry version 43.
DE   RecName: Full=Bacillolysin;
DE            EC=3.4.24.28;
DE   AltName: Full=Neutral protease;
DE   Flags: Precursor;
GN   Name=nprM; OrderedLocusNames=BMD_2285;
OS   Bacillus megaterium (strain DSM 319).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=592022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7764969; DOI=10.1007/BF00221230;
RA   Meinhardt F., Busskamp M., Wittchen K.D.;
RT   "Cloning and sequencing of the leu C and npr M genes and a putative
RT   spo IV gene from Bacillus megaterium DSM319.";
RL   Appl. Microbiol. Biotechnol. 41:344-351(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA   Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA   Vary P.S.;
RT   "Genome sequences of the industrial vitamin B12-producers B.
RT   megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT   genome evolution and pan-genome structure.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular zinc metalloprotease. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Similar, but not identical, to that of thermolysin.;
CC         EC=3.4.24.28;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 4 Ca(2+) ions per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
DR   EMBL; X75070; CAA52964.1; -; Genomic_DNA.
DR   EMBL; CP001982; ADF39133.1; -; Genomic_DNA.
DR   PIR; I40227; I40227.
DR   RefSeq; WP_013083132.1; NC_014103.1.
DR   SMR; D5DEH5; -.
DR   PRIDE; D5DEH5; -.
DR   EnsemblBacteria; ADF39133; ADF39133; BMD_2285.
DR   KEGG; bmd:BMD_2285; -.
DR   HOGENOM; HOG000247250; -.
DR   KO; K01400; -.
DR   OMA; HKRTTLA; -.
DR   OrthoDB; POG091H0APZ; -.
DR   BioCyc; BMEG592022:G1GHR-2279-MONOMER; -.
DR   Proteomes; UP000002365; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   CDD; cd09597; M4_neutral_protease; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR025711; PepSY.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF03413; PepSY; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Calcium; Complete proteome; Hydrolase; Metal-binding; Metalloprotease;
KW   Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25    245       Activation peptide. {ECO:0000255}.
FT                                /FTId=PRO_0000396525.
FT   CHAIN       246    562       Bacillolysin.
FT                                /FTId=PRO_0000396526.
FT   ACT_SITE    389    389       {ECO:0000250|UniProtKB:P05806}.
FT   ACT_SITE    477    477       Proton donor.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       303    303       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       305    305       Calcium 1.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       384    384       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       388    388       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       392    392       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       412    412       Zinc; catalytic.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       423    423       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       423    423       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       429    429       Calcium 3; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       431    431       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       431    431       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       433    433       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       436    436       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       436    436       Calcium 3.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       439    439       Calcium 4; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       440    440       Calcium 4.
FT                                {ECO:0000250|UniProtKB:P05806}.
FT   METAL       446    446       Calcium 4.
FT                                {ECO:0000250|UniProtKB:P05806}.
SQ   SEQUENCE   562 AA;  60862 MW;  BE1F088C0844F49A CRC64;
     MKKKKQALKV LLSVGILSSS FAFAHTSSAA PNNVLSTEKY NKEIKSPEFI SGKLSGPSSQ
     KAQDVVFHYM NTNKDKYKLG NENAQNSFKV TEVVKDPVEQ ATVVRLQQVY NNIPVWGSTQ
     LAHVAKDGTL KVVSGTVAPD LDKKEKLKGQ KQVDSKKAIQ AAEKDLGFKP TYEKSPSSEL
     YVYQNGSDTT YAYVVNLNFL SPEPGNYYYF VDAISGKVLD KYNTIDSVAG PKADVKQAAK
     PAAKPVTGTN AIGSGKGVLG DTKSLKTTLS SSTYYLQDNT RGATIYTYDA KNRTSLPGTL
     WTDTDNTYNA TRDAAAVDAH YYAGVTYDYY KNKFNRNSYD NAGAPLKSTV HYSSGYNNAF
     WNGSQMVYGD GDGTTFVPLS GGLDVIGHEL THAVTERSSN LIYQYESGAL NEAISDIFGT
     LVEYYDNRNP DWEIGEDIYT PGTSGDALRS MSNPAKYGDP DHYSKRYTGS SDNGGVHTNS
     GIINKAAYLL ANGGTHYGVT VTGIGGDKLG KIYYRANTLY FTQSTTFSQA RAGLVQAAAD
     LYGSGSQEVI SVGKSFDAVG VQ
//
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