LEPU_BACSU
ID LEPU_BACSU Reviewed; 187 AA.
AC P42959;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Signal peptidase I U;
DE Short=SPase I;
DE EC=3.4.21.89;
DE AltName: Full=Leader peptidase I;
GN Name=sipU; Synonyms=ycsB; OrderedLocusNames=BSU04010;
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;
RX PubMed=8574415; DOI=10.1099/13500872-141-12-3241;
RA Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA Yamane K.;
RT "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT region of the Bacillus subtilis chromosome and similarity analysis of the
RT products of putative ORFs.";
RL Microbiology 141:3241-3245(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
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 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 [5]
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 -!- 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 {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- INDUCTION: Expressed constitutively.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D38161; BAA07353.1; -; Genomic_DNA.
DR EMBL; D50453; BAA09032.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12209.1; -; Genomic_DNA.
DR PIR; I39890; I39890.
DR RefSeq; NP_388283.1; NC_000964.3.
DR RefSeq; WP_003234434.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P42959; -.
DR SMR; P42959; -.
DR STRING; 224308.BSU04010; -.
DR MEROPS; S26.005; -.
DR PaxDb; P42959; -.
DR PRIDE; P42959; -.
DR DNASU; 939966; -.
DR EnsemblBacteria; CAB12209; CAB12209; BSU_04010.
DR GeneID; 939966; -.
DR KEGG; bsu:BSU04010; -.
DR PATRIC; fig|224308.179.peg.426; -.
DR eggNOG; COG0681; Bacteria.
DR InParanoid; P42959; -.
DR OMA; CMVEGIS; -.
DR PhylomeDB; P42959; -.
DR BioCyc; BSUB:BSU04010-MON; -.
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..187
FT /note="Signal peptidase I U"
FT /id="PRO_0000109501"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 46
FT /evidence="ECO:0000250"
FT ACT_SITE 88
FT /evidence="ECO:0000250"
SQ SEQUENCE 187 AA; 21183 MW; 31C48774CF6A849B CRC64;
MNAKTITLKK KRKIKTIVVL SIIMIAALIF TIRLVFYKPF LIEGSSMAPT LKDSERILVD
KAVKWTGGFH RGDIIVIHDK KSGRSFVKRL IGLPGDSIKM KNDQLYINDK KVEEPYLKEY
KQEVKESGVT LTGDFEVEVP SGKYFVMGDN RLNSLDSRNG MGMPSEDDII GTESLVFYPF
GEMRQAK