(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 135.
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}.
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   SMR; P42959; -.
DR   STRING; 224308.BSU04010; -.
DR   MEROPS; S26.005; -.
DR   PaxDb; P42959; -.
DR   PRIDE; P42959; -.
DR   DNASU; 939966; -.
DR   EnsemblBacteria; CAB12209; CAB12209; BSU04010.
DR   GeneID; 939966; -.
DR   KEGG; bsu:BSU04010; -.
DR   PATRIC; fig|224308.179.peg.426; -.
DR   eggNOG; ENOG4108ZX0; Bacteria.
DR   eggNOG; COG0681; LUCA.
DR   HOGENOM; HOG000003673; -.
DR   InParanoid; P42959; -.
DR   KO; K03100; -.
DR   OMA; IEPRWIP; -.
DR   PhylomeDB; P42959; -.
DR   BioCyc; BSUB:BSU04010-MONOMER; -.
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   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; IPR015927; Peptidase_S24_S26A/B/C.
DR   Pfam; PF00717; Peptidase_S24; 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;
DR   PRODOM; P42959.
DR   SWISS-2DPAGE; P42959.
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
//

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