NPRB_BACSU
ID NPRB_BACSU Reviewed; 538 AA.
AC P39899;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Neutral protease B {ECO:0000303|PubMed:1917867};
DE EC=3.4.24.- {ECO:0000269|PubMed:1917867};
DE Flags: Precursor;
GN Name=nprB {ECO:0000303|PubMed:1917867}; OrderedLocusNames=BSU11100;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 224-228, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=1917867; DOI=10.1128/jb.173.20.6364-6372.1991;
RA Tran L., Wu X.C., Wong S.L.;
RT "Cloning and expression of a novel protease gene encoding an extracellular
RT neutral protease from Bacillus subtilis.";
RL J. Bacteriol. 173:6364-6372(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9025291; DOI=10.1099/00221287-143-1-175;
RA Levine A., Vannier F., Roche B., Autret S., Mavel D., Seror S.J.;
RT "A 10.3 kbp segment from nprB to argJ at the 102 degrees region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:175-177(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353931; DOI=10.1099/00221287-143-10-3305;
RA Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT degrees) in Bacillus subtilis.";
RL Microbiology 143:3305-3308(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
CC -!- FUNCTION: Protease able to cleave casein in vitro.
CC {ECO:0000269|PubMed:1917867}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:1917867};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:1917867};
CC -!- ACTIVITY REGULATION: Protease activity can be inhibited in vitro by
CC either a zinc specific chelator, 1,10-phenanthroline, or a metal
CC chelator, EDTA. The enzyme is resistant to phenylmethylsulfonyl
CC fluoride and iodoacetic acid. {ECO:0000269|PubMed:1917867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.6. {ECO:0000269|PubMed:1917867};
CC Temperature dependence:
CC Retains 65% activity after treatment at 65 degrees Celsius for 20
CC minutes. {ECO:0000269|PubMed:1917867};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1917867}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally in both LB
CC and SG media, and no difference in sporulation frequency can be
CC observed. {ECO:0000269|PubMed:1917867}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; M62845; AAA22626.1; -; Genomic_DNA.
DR EMBL; Z79580; CAB01832.1; -; Genomic_DNA.
DR EMBL; Y09476; CAA70628.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12950.1; -; Genomic_DNA.
DR PIR; A41042; A41042.
DR RefSeq; NP_388991.1; NC_000964.3.
DR RefSeq; WP_009966979.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39899; -.
DR SMR; P39899; -.
DR STRING; 224308.BSU11100; -.
DR MEROPS; M04.012; -.
DR PaxDb; P39899; -.
DR PRIDE; P39899; -.
DR EnsemblBacteria; CAB12950; CAB12950; BSU_11100.
DR GeneID; 936384; -.
DR KEGG; bsu:BSU11100; -.
DR PATRIC; fig|224308.179.peg.1192; -.
DR eggNOG; COG3227; Bacteria.
DR InParanoid; P39899; -.
DR OMA; TFDAENM; -.
DR PhylomeDB; P39899; -.
DR BioCyc; BSUB:BSU11100-MON; -.
DR Proteomes; UP000001570; 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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..223
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1917867"
FT /id="PRO_0000028608"
FT CHAIN 224..538
FT /note="Neutral protease B"
FT /id="PRO_0000028609"
FT REGION 421..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 453
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:1917867"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:1917867"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000305|PubMed:1917867"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 406
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 407
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 409
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 412
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 415
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 416
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 419
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
FT BINDING 422
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255"
SQ SEQUENCE 538 AA; 59336 MW; 4B7D2B8D8F64F14E CRC64;
MRNLTKTSLL LAGLCTAAQM VFVTHASAEE SIEYDHTYQT PSYIIEKSPQ KPVQNTTQKE
SLFSYLDKHQ TQFKLKGNAN SHFRVSKTIK DPKTKQTFFK LTEVYKGIPI YGFEQAVAMK
ENKQVKSFFG KVHPQIKDVS VTPSISEKKA IHTARRELEA SIGKIEYLDG EPKGELYIYP
HDGEYDLAYL VRLSTSEPEP GYWHYFIDAK NGKVIESFNA IHEAAGTGIG VSGDEKSFDV
TEQNGRFYLA DETRGKGINT FDAKNLNETL FTLLSQLIGY TGKEIVSGTS VFNEPAAVDA
HANAQAVYDY YSKTFGRDSF DQNGARITST VHVGKQWNNA AWNGVQMVYG DGDGSKFKPL
SGSLDIVAHE ITHAVTQYSA GLLYQGEPGA LNESISDIMG AMADRDDWEI GEDVYTPGIA
GDSLRSLEDP SKQGNPDHYS NRYTGTEDYG GVHINSSIHN KAAYLLAEGG VHHGVQVEGI
GREASEQIYY RALTYYVTAS TDFSMMKQAA IEAANDLYGE GSKQSASVEK AYEAVGIL
