LEPW_BACSU
ID LEPW_BACSU Reviewed; 190 AA.
AC P54506;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Signal peptidase I W;
DE Short=SPase I;
DE EC=3.4.21.89 {ECO:0000269|PubMed:9694797};
DE AltName: Full=Leader peptidase I;
GN Name=sipW {ECO:0000303|PubMed:9694797}; Synonyms=yqhE;
GN OrderedLocusNames=BSU24630;
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 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
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 [3]
RP CATALYTIC ACTIVITY, AND INDUCTION.
RX PubMed=9694797; DOI=10.1101/gad.12.15.2318;
RA Tjalsma H., Bolhuis A., van Roosmalen M.L., Wiegert T., Schumann W.,
RA Broekhuizen C.P., Quax W.J., Venema G., Bron S., van Dijl J.M.;
RT "Functional analysis of the secretory precursor processing machinery of
RT Bacillus subtilis: identification of a eubacterial homolog of archaeal and
RT eukaryotic signal peptidases.";
RL Genes Dev. 12:2318-2331(1998).
RN [4]
RP REVIEW.
RX PubMed=9823656; DOI=10.1016/s0168-1656(98)00099-6;
RA Bron S., Bolhuis A., Tjalsma H., Holsappel S., Venema G., van Dijl J.M.;
RT "Protein secretion and possible roles for multiple signal peptidases for
RT precursor processing in bacilli.";
RL J. Biotechnol. 64:3-13(1998).
RN [5]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=10049401; DOI=10.1128/jb.181.5.1664-1672.1999;
RA Stoever A.G., Driks A.;
RT "Secretion, localization, and antibacterial activity of TasA, a Bacillus
RT subtilis spore-associated protein.";
RL J. Bacteriol. 181:1664-1672(1999).
RN [6]
RP INDUCTION.
RX PubMed=10464223; DOI=10.1128/jb.181.17.5476-5481.1999;
RA Stoever A.G., Driks A.;
RT "Regulation of synthesis of the Bacillus subtilis transition-phase, spore-
RT associated antibacterial protein TasA.";
RL J. Bacteriol. 181:5476-5481(1999).
RN [7]
RP FUNCTION.
RX PubMed=10559173; DOI=10.1128/jb.181.22.7065-7069.1999;
RA Stoever A.G., Driks A.;
RT "Control of synthesis and secretion of the Bacillus subtilis protein
RT YqxM.";
RL J. Bacteriol. 181:7065-7069(1999).
RN [8]
RP FUNCTION, REPRESSION BY SINR, AND DISRUPTION PHENOTYPE.
RX PubMed=16430695; DOI=10.1111/j.1365-2958.2005.05019.x;
RA Chu F., Kearns D.B., Branda S.S., Kolter R., Losick R.;
RT "Targets of the master regulator of biofilm formation in Bacillus
RT subtilis.";
RL Mol. Microbiol. 59:1216-1228(2006).
RN [9]
RP INDUCTION BY REMA.
RX PubMed=23646920; DOI=10.1111/mmi.12235;
RA Winkelman J.T., Bree A.C., Bate A.R., Eichenberger P., Gourse R.L.,
RA Kearns D.B.;
RT "RemA is a DNA-binding protein that activates biofilm matrix gene
RT expression in Bacillus subtilis.";
RL Mol. Microbiol. 88:984-997(2013).
CC -!- FUNCTION: Required for the cleavage of the signal sequence of TasA and
CC TapA, which are involved in biofilm formation.
CC {ECO:0000269|PubMed:10049401, ECO:0000269|PubMed:10559173,
CC ECO:0000269|PubMed:16430695}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000269|PubMed:9694797};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Part of the tapA-sipW-tasA operon (PubMed:10464223).
CC Expression is directly repressed by the DNA-binding protein master
CC regulator of biofilm formation SinR and activated by the extracellular
CC matrix regulatory protein RemA (PubMed:16430695, PubMed:23646920).
CC Expressed constitutively at a low level (PubMed:9694797). Also
CC positively regulated by the sporulation transcription factors sigma H
CC and Spo0A and repressed by the transition phase regulatory protein
CC AbrB, probably indirectly (PubMed:10464223).
CC {ECO:0000269|PubMed:10464223, ECO:0000269|PubMed:16430695,
CC ECO:0000269|PubMed:23646920, ECO:0000269|PubMed:9694797}.
CC -!- DISRUPTION PHENOTYPE: Mutation impairs colony surface architecture.
CC {ECO:0000269|PubMed:16430695}.
CC -!- MISCELLANEOUS: B.subtilis contains five chromosomal type I signal
CC peptidases: SipS, SipT, SipU, SipV and SipW. They have different, but
CC overlapping, substrate specificities and have different transcription
CC patterns. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S26B family. {ECO:0000305}.
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DR EMBL; D84432; BAA12540.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14394.1; -; Genomic_DNA.
DR PIR; B69708; B69708.
DR RefSeq; NP_390343.1; NC_000964.3.
DR RefSeq; WP_003246088.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P54506; -.
DR STRING; 224308.BSU24630; -.
DR MEROPS; S26.011; -.
DR PaxDb; P54506; -.
DR PRIDE; P54506; -.
DR EnsemblBacteria; CAB14394; CAB14394; BSU_24630.
DR GeneID; 938542; -.
DR KEGG; bsu:BSU24630; -.
DR PATRIC; fig|224308.43.peg.2570; -.
DR eggNOG; COG0681; Bacteria.
DR InParanoid; P54506; -.
DR OMA; VITFMQD; -.
DR PhylomeDB; P54506; -.
DR BioCyc; BSUB:BSU24630-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR019533; Peptidase_S26.
DR InterPro; IPR001733; Peptidase_S26B.
DR InterPro; IPR027245; Sec11.
DR PANTHER; PTHR10806; PTHR10806; 1.
DR PANTHER; PTHR10806:SF6; PTHR10806:SF6; 1.
DR PRINTS; PR00728; SIGNALPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02228; sigpep_I_arch; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..190
FT /note="Signal peptidase I W"
FT /id="PRO_0000109539"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 45
FT /evidence="ECO:0000250"
SQ SEQUENCE 190 AA; 20678 MW; 0F3FBD2F08D2BB3C CRC64;
MKLISNILYV IIFTLIIVLT LVVISTRSSG GEPAVFGYTL KSVLSGSMEP EFNTGSLILV
KEITDVKELQ KGDVITFMQD ANTAVTHRIV DITKQGDHLL FKTKGDNNAA ADSAPVSDEN
VRAQYTGFQL PYAGYMLHFA SQPIGTAVLL IVPGVMLLVY AFVTISSAIR EIERKTKALE
TDTKDSTMST
