ID   SPPA_ALKHC              Reviewed;         331 AA.
AC   Q9K809;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative signal peptide peptidase SppA;
DE            EC=3.4.21.-;
GN   Name=sppA; OrderedLocusNames=BH3198;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: Digestion of the cleaved signal peptides. {ECO:0000250}.
CC   -!- SUBUNIT: Homooctamer, assembles into a ring structure with a central
CC       cavity. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB06917.1; -; Genomic_DNA.
DR   PIR; F84049; F84049.
DR   AlphaFoldDB; Q9K809; -.
DR   SMR; Q9K809; -.
DR   STRING; 272558.10175821; -.
DR   EnsemblBacteria; BAB06917; BAB06917; BAB06917.
DR   KEGG; bha:BH3198; -.
DR   eggNOG; COG0616; Bacteria.
DR   HOGENOM; CLU_046540_0_1_9; -.
DR   OMA; CDELWAR; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW   Serine protease; Transmembrane; Transmembrane helix.
FT   CHAIN           1..331
FT                   /note="Putative signal peptide peptidase SppA"
FT                   /id="PRO_0000171441"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        145
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        197
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   331 AA;  36104 MW;  F3A4DE8FF64EB152 CRC64;
     MMSRKRWLAL IAAAMLFVAS AAISLVSSPA VDVDEWVGTG TSYKQTIVET GTDFGKSIAI
     LELSGVIQDT GSAPSLLNTG VYHHRDFLKQ LEKAGEDPNI AGIILQVNTP GGGVLESAEI
     HKQVEEIVQD SEKPVYVSMG NMAASGGYYI SAPATKIYAH PQTITGSIGV IMQSIDISGL
     AENLGIEFNT FKSGPYKDIL SQTREVTDEE EDILQTLVDE MYDEFVRVIV DGRGMSETEV
     RELADGRIYT GSQAVATGLV DELGGLDDVI ESMKEDLGAD YNVIRYEHSL GLYDFFSMST
     NRLLSPSYEL QSIERLLNQS NTPTLQYLYA E