ID   LEPV_BACSU              Reviewed;         168 AA.
AC   O07560;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Signal peptidase I V;
DE            Short=SPase I;
DE            EC=3.4.21.89;
DE   AltName: Full=Leader peptidase I;
GN   Name=sipV; Synonyms=yhjF; OrderedLocusNames=BSU10490;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA   Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA   Venema G., Bron S.;
RT   "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT   subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT   many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL   Microbiology 144:859-875(1998).
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   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}.
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DR   EMBL; Y14081; CAA74468.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12889.1; -; Genomic_DNA.
DR   PIR; A69708; A69708.
DR   RefSeq; NP_388930.1; NC_000964.3.
DR   RefSeq; WP_003233128.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O07560; -.
DR   SMR; O07560; -.
DR   STRING; 224308.BSU10490; -.
DR   MEROPS; S26.006; -.
DR   PaxDb; 224308-BSU10490; -.
DR   DNASU; 939318; -.
DR   EnsemblBacteria; CAB12889; CAB12889; BSU_10490.
DR   GeneID; 939318; -.
DR   KEGG; bsu:BSU10490; -.
DR   PATRIC; fig|224308.179.peg.1128; -.
DR   eggNOG; COG0681; Bacteria.
DR   InParanoid; O07560; -.
DR   OrthoDB; 9802919at2; -.
DR   PhylomeDB; O07560; -.
DR   BioCyc; BSUB:BSU10490-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 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   NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR   PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR   PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR   Pfam; PF10502; Peptidase_S26; 1.
DR   PRINTS; PR00727; LEADERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR   PROSITE; PS00501; SPASE_I_1; 1.
DR   PROSITE; PS00760; SPASE_I_2; 1.
DR   PROSITE; PS00761; SPASE_I_3; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..168
FT                   /note="Signal peptidase I V"
FT                   /id="PRO_0000109502"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..168
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        34
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        75
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   168 AA;  18956 MW;  D70BD09545638604 CRC64;
     MKKRFWFLAG VVSVVLAIQV KNAVFIDYKV EGVSMNPTFQ EGNELLVNKF SHRFKTIHRF
     DIVLFKGPDH KVLIKRVIGL PGETIKYKDD QLYVNGKQVA EPFLKHLKSV SAGSHVTGDF
     SLKDVTGTSK VPKGKYFVVG DNRIYSFDSR HFGPIREKNI VGVISDAE
//