SUBE_BACSU
ID SUBE_BACSU Reviewed; 645 AA.
AC P16396;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Minor extracellular protease Epr;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN Name=epr; OrderedLocusNames=BSU38400; ORFNames=ipa-15r;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / DB204;
RX PubMed=2116590; DOI=10.1007/bf00259415;
RA Brueckner R., Shoseyov O., Doi R.H.;
RT "Multiple active forms of a novel serine protease from Bacillus subtilis.";
RL Mol. Gen. Genet. 221:486-490(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3142851; DOI=10.1128/jb.170.12.5557-5563.1988;
RA Sloma A., Ally A., Ally D., Pero J.;
RT "Gene encoding a minor extracellular protease in Bacillus subtilis.";
RL J. Bacteriol. 170:5557-5563(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
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).
RN [5]
RP REGULATION BY HPR AND SINR.
RC STRAIN=168;
RX PubMed=16923912; DOI=10.1128/jb.00427-06;
RA Kodgire P., Dixit M., Rao K.K.;
RT "ScoC and SinR negatively regulate epr by corepression in Bacillus
RT subtilis.";
RL J. Bacteriol. 188:6425-6428(2006).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- INDUCTION: Negatively regulated jointly by Hpr and SinR, which bind to
CC their respective target sites 62 bp apart.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; X53307; CAA37392.1; -; Genomic_DNA.
DR EMBL; M22407; AAA22423.1; -; Genomic_DNA.
DR EMBL; X73124; CAA51571.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15866.1; -; Genomic_DNA.
DR PIR; S11504; SUBSMP.
DR RefSeq; NP_391719.1; NC_000964.3.
DR RefSeq; WP_003243950.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P16396; -.
DR SMR; P16396; -.
DR STRING; 224308.BSU38400; -.
DR MEROPS; S08.126; -.
DR PaxDb; P16396; -.
DR PRIDE; P16396; -.
DR EnsemblBacteria; CAB15866; CAB15866; BSU_38400.
DR GeneID; 937332; -.
DR KEGG; bsu:BSU38400; -.
DR PATRIC; fig|224308.179.peg.4157; -.
DR eggNOG; COG1404; Bacteria.
DR InParanoid; P16396; -.
DR OMA; IGAKHNG; -.
DR PhylomeDB; P16396; -.
DR BioCyc; BSUB:BSU38400-MON; -.
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 GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 1.10.10.1270; -; 4.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR041909; Sbi_C3_db_domIV.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..103
FT /evidence="ECO:0000255"
FT /id="PRO_0000027170"
FT CHAIN 104..645
FT /note="Minor extracellular protease Epr"
FT /id="PRO_0000027171"
FT DOMAIN 115..382
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 490..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 172
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 645 AA; 69696 MW; 401A4D5B60BE2E4A CRC64;
MKNMSCKLVV SVTLFFSFLT IGPLAHAQNS SEKEVIVVYK NKAGKETILD SDADVEQQYK
HLPAVAVTAD QETVKELKQD PDILYVENNV SFTAADSTDF KVLSDGTDTS DNFEQWNLEP
IQVKQAWKAG LTGKNIKIAV IDSGISPHDD LSIAGGYSAV SYTSSYKDDN GHGTHVAGII
GAKHNGYGID GIAPEAQIYA VKALDQNGSG DLQSLLQGID WSIANRMDIV NMSLGTTSDS
KILHDAVNKA YEQGVLLVAA SGNDGNGKPV NYPAAYSSVV AVSATNEKNQ LASFSTTGDE
VEFSAPGTNI TSTYLNQYYA TGSGTSQATP HAAAMFALLK QRDPAETNVQ LREEMRKNIV
DLGTAGRDQQ FGYGLIQYKA QATDSAYAAA EQAVKKAEQT KAQIDINKAR ELISQLPNSD
AKTALHKRLD KVQSYRNVKD AKDKVAKAEK YKTQQTVDTA QTAINKLPNG TDKKNLQKRL
DQVKRYIASK QAKDKVAKAE KSKKKTDVDS AQSAIGKLPA SSEKTSLQKR LNKVKSTNLK
TAQQSVSAAE KKSTDANAAK AQSAVNQLQA GKDKTALQKR LDKVKKKVAA AEAKKVETAK
AKVKKAEKDK TKKSKTSAQS AVNQLKASNE KTKLQKRLNA VKPKK
