SPPA_BACSU
ID SPPA_BACSU Reviewed; 335 AA.
AC O34525;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Putative signal peptide peptidase SppA;
DE EC=3.4.21.-;
GN Name=sppA; Synonyms=yteI; OrderedLocusNames=BSU29530;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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 FUNCTION.
RC STRAIN=168;
RX PubMed=10455123; DOI=10.1074/jbc.274.35.24585;
RA Bolhuis A., Matzen A., Hyyrylaeinen H.-L., Kontinen V.P., Meima R.,
RA Chapuis J., Venema G., Bron S., Freudl R., van Dijl J.M.;
RT "Signal peptide peptidase- and ClpP-like proteins of Bacillus subtilis
RT required for efficient translocation and processing of secretory
RT proteins.";
RL J. Biol. Chem. 274:24585-24592(1999).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 56-295, SUBUNIT, MUTAGENESIS OF
RP SER-147 AND LYS-199, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=22472423; DOI=10.1016/j.jmb.2012.03.020;
RA Nam S.E., Kim A.C., Paetzel M.;
RT "Crystal structure of Bacillus subtilis signal peptide peptidase A.";
RL J. Mol. Biol. 419:347-358(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.39 ANGSTROMS) OF 51-335, SUBUNIT, AUTOCATALYTIC
RP CLEAVAGE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF LYS-199.
RX PubMed=24228759; DOI=10.1021/bi4011489;
RA Nam S.E., Paetzel M.;
RT "Structure of signal peptide peptidase A with C-termini bound in the active
RT sites: insights into specificity, self-processing, and regulation.";
RL Biochemistry 52:8811-8822(2013).
CC -!- FUNCTION: Digestion of cleaved signal peptides (By similarity).
CC Required for efficient processing of precursors under conditions of
CC hyper-secretion. Has a preference for leucine-rich substrate peptides.
CC {ECO:0000250, ECO:0000269|PubMed:10455123}.
CC -!- SUBUNIT: Homooctamer, assembles into a ring structure with a central
CC cavity (PubMed:22472423, PubMed:24228759). Interacts with FloT
CC (PubMed:23651456). {ECO:0000269|PubMed:22472423,
CC ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:24228759}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456,
CC ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Single-pass membrane protein.
CC Note=Present in detergent-resistant membrane (DRM) fractions that may
CC be equivalent to eukaryotic membrane rafts; these rafts include
CC proteins involved in signaling, molecule trafficking and protein
CC secretion. {ECO:0000269|PubMed:23651456}.
CC -!- PTM: Autocatalytically cleaves its own C-terminus.
CC -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}.
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DR EMBL; AF008220; AAC00312.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14931.1; -; Genomic_DNA.
DR PIR; E69990; E69990.
DR RefSeq; NP_390831.1; NC_000964.3.
DR RefSeq; WP_003229337.1; NZ_JNCM01000036.1.
DR PDB; 3RST; X-ray; 2.37 A; A/B/C/D/E/F/G/H=56-295.
DR PDB; 4KWB; X-ray; 2.39 A; A/B/C/D/E/F/G/H=51-335.
DR PDBsum; 3RST; -.
DR PDBsum; 4KWB; -.
DR AlphaFoldDB; O34525; -.
DR SMR; O34525; -.
DR STRING; 224308.BSU29530; -.
DR MEROPS; S49.008; -.
DR jPOST; O34525; -.
DR PaxDb; O34525; -.
DR DNASU; 937679; -.
DR EnsemblBacteria; CAB14931; CAB14931; BSU_29530.
DR GeneID; 937679; -.
DR KEGG; bsu:BSU29530; -.
DR PATRIC; fig|224308.179.peg.3208; -.
DR eggNOG; COG0616; Bacteria.
DR InParanoid; O34525; -.
DR OMA; CDELWAR; -.
DR PhylomeDB; O34525; -.
DR BioCyc; BSUB:BSU29530-MON; -.
DR BRENDA; 3.4.23.B24; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR004635; Pept_S49_SppA.
DR InterPro; IPR002142; Peptidase_S49.
DR Pfam; PF01343; Peptidase_S49; 1.
DR SUPFAM; SSF52096; SSF52096; 1.
DR TIGRFAMs; TIGR00706; SppA_dom; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Membrane; Protease;
KW Reference proteome; Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..335
FT /note="Putative signal peptide peptidase SppA"
FT /id="PRO_0000171442"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:22472423"
FT ACT_SITE 199
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:22472423"
FT SITE 294..295
FT /note="Cleavage; by autolysis"
FT MUTAGEN 147
FT /note="S->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22472423"
FT MUTAGEN 199
FT /note="K->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:22472423,
FT ECO:0000269|PubMed:24228759"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4KWB"
FT HELIX 116..133
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:3RST"
FT TURN 197..202
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 210..235
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 253..258
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 261..265
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:3RST"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:3RST"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:4KWB"
SQ SEQUENCE 335 AA; 36673 MW; 10BDA2DF8527D28B CRC64;
MNAKRWIALV IALGIFGVSI IVSISMSFFE SVKGAQTDLT SLTDESQEKT LENGSPSSKI
AVLEVSGTIQ DNGDSSSLLG ADGYNHRTFL KNLERAKDDK TVKGIVLKVN SPGGGVYESA
EIHKKLEEIK KETKKPIYVS MGSMAASGGY YISTAADKIF ATPETLTGSL GVIMESVNYS
KLADKLGISF ETIKSGAHKD IMSPSREMTK EEKNIMQSMV DNSYEGFVDV ISKGRGMPKA
EVKKIADGRV YDGRQAKKLN LVDELGFYDD TITAMKKDHK DLKNASVISY EESFGLGSLF
SMGANKMFKS EIDFLNMREI LSQSGSPRMM YLYAK
