LEPS_BACSU
ID LEPS_BACSU Reviewed; 184 AA.
AC P28628;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Signal peptidase I S;
DE Short=SPase I;
DE EC=3.4.21.89;
DE AltName: Full=Leader peptidase I;
GN Name=sipS; OrderedLocusNames=BSU23310;
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 / 6GM(AMY);
RX PubMed=1639057;
RA van Dijl J.M., de Jong A., Vehmaanpera J., Venema G., Bron S.;
RT "Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids
RT in prokaryotic and eukaryotic type I signal peptidases.";
RL EMBO J. 11:2819-2828(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT "The organization of the Bacillus subtilis 168 chromosome region between
RT the spoVA and serA genetic loci, based on sequence data.";
RL Mol. Microbiol. 10:385-395(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
RX PubMed=7876097; DOI=10.1074/jbc.270.8.3611;
RA van Dijl J.M., de Jong A., Venema G., Bron S.;
RT "Identification of the potential active site of the signal peptidase SipS
RT of Bacillus subtilis. Structural and functional similarities with LexA-like
RT proteases.";
RL J. Biol. Chem. 270:3611-3618(1995).
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 CHARACTERIZATION.
RX PubMed=8951809; DOI=10.1046/j.1365-2958.1996.d01-4676.x;
RA Bolhuis A., Sorokin A., Azevedo V., Ehrlich S.D., Braun P.G., de Jong A.,
RA Venema G., Bron S., van Dijl J.M.;
RT "Bacillus subtilis can modulate its capacity and specificity for protein
RT secretion through temporally controlled expression of the sipS gene for
RT signal peptidase I.";
RL Mol. Microbiol. 22:605-618(1996).
RN [6]
RP CHARACTERIZATION.
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 [7]
RP FUNCTION OF TRANSMEMBRANE DOMAIN.
RX PubMed=10982814; DOI=10.1074/jbc.m007093200;
RA Carlos J.L., Paetzel M., Brubaker G., Karla A., Ashwell C.M., Lively M.O.,
RA Cao G., Bullinger P., Dalbey R.E.;
RT "The role of the membrane-spanning domain of type I signal peptidases in
RT substrate cleavage site selection.";
RL J. Biol. Chem. 275:38813-38822(2000).
RN [8]
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).
CC -!- FUNCTION: Not essential for cell viability, but required for efficient
CC secretion of many proteins. {ECO:0000269|PubMed:10982814}.
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 -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- INDUCTION: Expressed at the postexponential growth phase; regulated by
CC the DegS-DegU system.
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.
CC -!- SIMILARITY: Belongs to the peptidase S26 family. {ECO:0000305}.
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DR EMBL; Z11847; CAA77871.1; -; Genomic_DNA.
DR EMBL; L09228; AAA67478.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14263.1; -; Genomic_DNA.
DR PIR; S23381; S23381.
DR RefSeq; NP_390212.1; NC_000964.3.
DR RefSeq; WP_003246166.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P28628; -.
DR SMR; P28628; -.
DR STRING; 224308.BSU23310; -.
DR MEROPS; S26.003; -.
DR PaxDb; P28628; -.
DR PRIDE; P28628; -.
DR DNASU; 938944; -.
DR EnsemblBacteria; CAB14263; CAB14263; BSU_23310.
DR GeneID; 938944; -.
DR KEGG; bsu:BSU23310; -.
DR PATRIC; fig|224308.179.peg.2537; -.
DR eggNOG; COG0681; Bacteria.
DR InParanoid; P28628; -.
DR OMA; IEPRWIP; -.
DR PhylomeDB; P28628; -.
DR BioCyc; BSUB:BSU23310-MON; -.
DR BRENDA; 3.4.21.89; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006465; P:signal peptide processing; IBA:GO_Central.
DR CDD; cd06530; S26_SPase_I; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019756; Pept_S26A_signal_pept_1_Ser-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR PANTHER; PTHR43390; PTHR43390; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; SSF51306; 1.
DR TIGRFAMs; TIGR02227; sigpep_I_bact; 1.
DR PROSITE; PS00501; SPASE_I_1; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..184
FT /note="Signal peptidase I S"
FT /id="PRO_0000109499"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 43
FT ACT_SITE 83
FT MUTAGEN 42
FT /note="D->S: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 43
FT /note="S->A,V: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 43
FT /note="S->C,T: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 44
FT /note="M->A: Increased activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 46
FT /note="P->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 47
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 48
FT /note="L->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 69
FT /note="G->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 70
FT /note="D->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 71
FT /note="I->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 72
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 74
FT /note="L->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 79
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 81
FT /note="Y->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 81
FT /note="Y->F: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 83
FT /note="K->A,H,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 84
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 84
FT /note="R->H: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 84
FT /note="R->K: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 86
FT /note="I->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 87
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 88
FT /note="L->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 89
FT /note="P->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 90
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 91
FT /note="D->A,E,N: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 141
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 145
FT /note="G->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 146
FT /note="D->A,N: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 146
FT /note="D->E: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 147
FT /note="N->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 150
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 151
FT /note="S->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 153
FT /note="D->A: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 153
FT /note="D->E,N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 154
FT /note="S->A: Slightly reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
FT MUTAGEN 155
FT /note="R->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:7876097"
SQ SEQUENCE 184 AA; 21047 MW; 5A2D005BF0D33CE9 CRC64;
MKSENVSKKK SILEWAKAIV IAVVLALLIR NFIFAPYVVD GDSMYPTLHN RERVFVNMTV
KYIGEFDRGD IVVLNGDDVH YVKRIIGLPG DTVEMKNDQL YINGKKVDEP YLAANKKRAK
QDGFDHLTDD FGPVKVPDNK YFVMGDNRRN SMDSRNGLGL FTKKQIAGTS KFVFYPFNEM
RKTN
