WPRA_BACSU
ID WPRA_BACSU Reviewed; 894 AA.
AC P54423; O06726;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Cell wall-associated protease;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Cell wall-associated polypeptide CWBP23;
DE Short=CWBP23;
DE Contains:
DE RecName: Full=Cell wall-associated polypeptide CWBP52;
DE Short=CWBP52;
DE Flags: Precursor;
GN Name=wprA; Synonyms=yisM; OrderedLocusNames=BSU10770;
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 32-54 AND 414-428,
RP FUNCTION AS A PROTEASE, ACTIVITY REGULATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9004506; DOI=10.1099/13500872-142-12-3437;
RA Margot P., Karamata D.;
RT "The wprA gene of Bacillus subtilis 168, expressed during exponential
RT growth, encodes a cell-wall-associated protease.";
RL Microbiology 142:3437-3444(1996).
RN [2]
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 [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 PROTEIN SEQUENCE OF 32-41 AND 414-424, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=10658653; DOI=10.1099/00221287-146-1-65;
RA Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.;
RT "Proteome analysis of Bacillus subtilis extracellular proteins: a two-
RT dimensional protein electrophoretic study.";
RL Microbiology 146:65-75(2000).
RN [5]
RP INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=11987133;
RX DOI=10.1002/1615-9861(200205)2:5<591::aid-prot591>3.0.co;2-8;
RA Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.;
RT "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic
RT approach.";
RL Proteomics 2:591-602(2002).
CC -!- FUNCTION: CWBP52 is a serine-type protease that could be involved in
CC proteoglycan peptide bridges. {ECO:0000269|PubMed:9004506}.
CC -!- ACTIVITY REGULATION: Inhibited by PMSF. {ECO:0000269|PubMed:9004506}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10658653,
CC ECO:0000269|PubMed:11987133}. Note=Released into the medium.
CC -!- INDUCTION: In stationary phase. {ECO:0000269|PubMed:11987133}.
CC -!- PTM: Proteolytically cleaved to yield CWBP23 and CWBP52.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no discernible
CC phenotype with respect to sporulation, motility or growth
CC (PubMed:9004506). Significantly increased amounts of BglS, Epr, Vpr,
CC YclQ and YwsB; decreased amounts of AbnA, PorE, Csn, YncM, Yxal and
CC YweA are detected in the extracellular proteome (PubMed:11987133).
CC {ECO:0000269|PubMed:11987133, ECO:0000269|PubMed:9004506}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- CAUTION: The CWBP52 polypeptide was originally called CWBP55 based on
CC its apparent molecular weight. {ECO:0000305}.
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DR EMBL; U58981; AAC25926.1; -; Genomic_DNA.
DR EMBL; Y09476; CAA70641.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12917.1; -; Genomic_DNA.
DR PIR; F69730; F69730.
DR RefSeq; NP_388958.1; NC_000964.3.
DR RefSeq; WP_003244653.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P54423; -.
DR SMR; P54423; -.
DR IntAct; P54423; 15.
DR STRING; 224308.BSU10770; -.
DR MEROPS; S08.004; -.
DR jPOST; P54423; -.
DR PaxDb; P54423; -.
DR PRIDE; P54423; -.
DR EnsemblBacteria; CAB12917; CAB12917; BSU_10770.
DR GeneID; 936350; -.
DR KEGG; bsu:BSU10770; -.
DR PATRIC; fig|224308.179.peg.1158; -.
DR eggNOG; COG1404; Bacteria.
DR InParanoid; P54423; -.
DR OMA; YYKAAPF; -.
DR BioCyc; BSUB:BSU10770-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07484; Peptidases_S8_Thermitase_like; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR041498; Big_6.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034084; Thermitase-like_dom.
DR Pfam; PF17936; Big_6; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Hydrolase; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:10658653,
FT ECO:0000269|PubMed:9004506"
FT CHAIN 32..894
FT /note="Cell wall-associated protease"
FT /id="PRO_0000027197"
FT CHAIN 32..?
FT /note="Cell wall-associated polypeptide CWBP23"
FT /id="PRO_0000027198"
FT PROPEP ?..413
FT /evidence="ECO:0000255"
FT /id="PRO_0000027199"
FT CHAIN 414..894
FT /note="Cell wall-associated polypeptide CWBP52"
FT /id="PRO_0000027200"
FT DOMAIN 422..729
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 462
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 497
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 650
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CONFLICT 9
FT /note="V -> A (in Ref. 1; AAC25926)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="L -> I (in Ref. 1; AAC25926)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 894 AA; 96488 MW; 0F67C353E55F8DBC CRC64;
MKRRKFSSVV AAVLIFALIF SLFSPGTKAA AAGAIDQAAA LENGKEQTGA MKEPEQVKWY
KVTPGATDIQ KNSHMALTVK SDSVLNVSVY PSKEKALKDE TFEMYRSFTA EDGKSEVIFP
YAWSGPYYVK VEYLGEEEPE DGGTAEAAAE AKYTIGYKGT KKQPSDLEEE EACPVEMSVD
QKKSGKGILD KLRSIRDEQL SQTAEGKELT SLYYKAAPFI VAKLALNKTA RNEIYQDLVT
LKPLFDDVSE NGASSSYKVT EKDQKAINRL YDKALQSVPS FLKEEIKKQA DRLNMKQLQG
KTAGAILTEN NIAAKSEVQT TKVIFKVKDN KSLSSVHNEM KGFSASAQSK KDISNVKKAK
KLFDNLYSFE LPKDEKQNGA YTASAKRVKS AAATLSKMSN VEFAEPVQEY KSLANDIQYP
YQWPLKNNGE NGGVKNADVK YEPANTLLSK RKLNDTLIAV VDTGVDSTLA DLKGKVRTDL
GHNFVGRNNN AMDDQGHGTH VAGIIAAQSD NGYSMTGLNA KAKIIPVKVL DSAGSGDTEQ
IALGIKYAAD KGAKVINLSL GGGYSRVLEF ALKYAADKNV LIAAASGNDG ENALSYPASS
KYVMSVGATN RMDMTADFSN YGKGLDISAP GSDIPSLVPN GNVTYMSGTS MATPYAAAAA
GLLFAQNPKL KRTEVEDMLK KTADDISFES VDGGEEELYD DYGDPIEIPK TPGVDWHSGY
GRLNVMKAVS AADLQLKVNK LESTQTAVRG SAKEGTLIEV MNGKKKLGSA KAGKDNAFKV
NIATQKQDQV LYLKATKGDA KTSYKVVVVK GKPSGTPKVN AVKTKDTAVK GKANSKAMIR
VKNKSKKVIA SAKADAKGTF SVKIKKQKAG TVLYVTAVDT DKKESKEAKV VVEK
