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Database: UniProt
Entry: F3UEY8_STRSA
LinkDB: F3UEY8_STRSA
Original site: F3UEY8_STRSA 
ID   F3UEY8_STRSA            Unreviewed;       209 AA.
AC   F3UEY8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
DE            EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU003993};
GN   Name=spi {ECO:0000313|EMBL:EGJ35982.1};
GN   ORFNames=HMPREF9393_2192 {ECO:0000313|EMBL:EGJ35982.1};
OS   Streptococcus sanguinis SK1056.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=888820 {ECO:0000313|EMBL:EGJ35982.1, ECO:0000313|Proteomes:UP000004171};
RN   [1] {ECO:0000313|EMBL:EGJ35982.1, ECO:0000313|Proteomes:UP000004171}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK1056 {ECO:0000313|EMBL:EGJ35982.1,
RC   ECO:0000313|Proteomes:UP000004171};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000677,
CC         ECO:0000256|RuleBase:RU003993};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606,
CC       ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGJ35982.1}.
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DR   EMBL; AFFL01000009; EGJ35982.1; -; Genomic_DNA.
DR   RefSeq; WP_002923173.1; NZ_GL890990.1.
DR   AlphaFoldDB; F3UEY8; -.
DR   MEROPS; S26.015; -.
DR   PATRIC; fig|888820.3.peg.2142; -.
DR   HOGENOM; CLU_028723_5_0_9; -.
DR   Proteomes; UP000004171; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
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; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993, ECO:0000313|EMBL:EGJ35982.1};
KW   Membrane {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Transmembrane {ECO:0000256|RuleBase:RU003993};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT   TRANSMEM        14..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003993"
FT   DOMAIN          12..201
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   209 AA;  24021 MW;  63CB61326747602A CRC64;
     MKKSNTAVVI LKEWGLFIIF ISVIILSRLY LWSPVKVDGH SMDPTLANGE YLLVLKYQSI
     DRFDIVVATE TDKDGTTKEI VKRVIGMPGD TIQYENDTLY INGKKTDEPY LTDYIKKFKE
     DKLQSTYTGD DYDDNGVFFR KLAAQAQAFT VDSEGSPVFT IKLLDDEYLL LGDDRIVSKD
     SRQVGTFQKE QIHGEAKFRF WPLLPFKTY
//
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