(data stored in SCRATCH zone)

SWISSPROT: MPR_BACSU

ID   MPR_BACSU               Reviewed;         313 AA.
AC   P39790;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   11-DEC-2019, entry version 120.
DE   RecName: Full=Extracellular metalloprotease;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=mpr; OrderedLocusNames=BSU02240;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=GP241;
RX   PubMed=2105291; DOI=10.1128/jb.172.2.1024-1029.1990;
RA   Sloma A., Rudolph C.F., Rufo G.A. Jr., Sullivan B.J., Theriault K.A.,
RA   Ally D., Pero J.;
RT   "Gene encoding a novel extracellular metalloprotease in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 172:1024-1029(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
RX   PubMed=3145906; DOI=10.1016/0378-1119(88)90207-7;
RA   Smith H., de Jong A., Bron S., Venema G.;
RT   "Characterization of signal-sequence-coding regions selected from the
RT   Bacillus subtilis chromosome.";
RL   Gene 70:351-361(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC   STRAIN=168;
RX   PubMed=7496533; DOI=10.1099/13500872-141-9-2211;
RA   Saxild H.H., Jacobsen J.H., Nygaard P.;
RT   "Functional analysis of the Bacillus subtilis purT gene encoding formate-
RT   dependent glycinamide ribonucleotide transformylase.";
RL   Microbiology 141:2211-2218(1995).
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase S1B family. {ECO:0000305}.
CC   -!- CAUTION: Called 'metalloprotease', but clearly belongs to the S1B
CC       family of serine proteases. {ECO:0000305}.
DR   EMBL; L10505; AAA22604.1; -; Genomic_DNA.
DR   EMBL; AB006424; BAA33121.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12018.1; -; Genomic_DNA.
DR   EMBL; M22916; AAA22832.1; -; Genomic_DNA.
DR   PIR; A35122; A35122.
DR   RefSeq; NP_388106.1; NC_000964.3.
DR   RefSeq; WP_003246370.1; NZ_JNCM01000030.1.
DR   STRING; 224308.BSU02240; -.
DR   MEROPS; S01.272; -.
DR   PaxDb; P39790; -.
DR   PRIDE; P39790; -.
DR   DNASU; 938430; -.
DR   EnsemblBacteria; CAB12018; CAB12018; BSU02240.
DR   GeneID; 938430; -.
DR   KEGG; bsu:BSU02240; -.
DR   PATRIC; fig|224308.179.peg.230; -.
DR   eggNOG; ENOG4108TCS; Bacteria.
DR   eggNOG; COG3591; LUCA.
DR   HOGENOM; HOG000221555; -.
DR   InParanoid; P39790; -.
DR   OMA; TYGCQSG; -.
DR   PhylomeDB; P39790; -.
DR   BioCyc; BSUB:BSU02240-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR008256; Peptidase_S1B.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
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;
DR   PRODOM; P39790.
DR   SWISS-2DPAGE; P39790.
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW   Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..93
FT                   /id="PRO_0000026902"
FT   CHAIN           94..313
FT                   /note="Extracellular metalloprotease"
FT                   /id="PRO_0000026903"
FT   ACT_SITE        146
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT   ACT_SITE        267
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10083"
FT   DISULFID        131..147
FT                   /evidence="ECO:0000250"
FT   CONFLICT        61..68
FT                   /note="QVSAPYEG -> PLESTAQA (in Ref. 4; AAA22832)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   313 AA;  33842 MW;  D41788E8D652AE94 CRC64;
     MKLVPRFRKQ WFAYLTVLCL ALAAAVSFGV PAKAAENPQT SVSNTGKEAD ATKNQTSKAD
     QVSAPYEGTG KTSKSLYGGQ TELEKNIQTL QPSSIIGTDE RTRISSTTSF PYRATVQLSI
     KYPNTSSTYG CTGFLVNPNT VVTAGHCVYS QDHGWASTIT AAPGRNGSSY PYGTYSGTMF
     YSVKGWTESK DTNYDYGAIK LNGSPGNTVG WYGYRTTNSS SPVGLSSSVT GFPCDKTFGT
     MWSDTKPIRS AETYKLTYTT DTYGCQSGSP VYRNYSDTGQ TAIAIHTNGG SSYNLGTRVT
     NDVFNNIQYW ANQ
//

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