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Database: UniProt
Entry: A0A1I6A746_9BACI
LinkDB: A0A1I6A746_9BACI
Original site: A0A1I6A746_9BACI 
ID   A0A1I6A746_9BACI        Unreviewed;       185 AA.
AC   A0A1I6A746;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
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   ORFNames=SAMN04488577_0715 {ECO:0000313|EMBL:SFQ64564.1};
OS   Bacillus sp. cl95.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761761 {ECO:0000313|EMBL:SFQ64564.1, ECO:0000313|Proteomes:UP000199578};
RN   [1] {ECO:0000313|EMBL:SFQ64564.1, ECO:0000313|Proteomes:UP000199578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CL95 {ECO:0000313|EMBL:SFQ64564.1,
RC   ECO:0000313|Proteomes:UP000199578};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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|RuleBase:RU362042}; Single-pass type II membrane
CC       protein {ECO:0000256|RuleBase:RU362042}.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; FOYF01000001; SFQ64564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6A746; -.
DR   STRING; 1761761.SAMN04488577_0715; -.
DR   OrthoDB; 9802919at2; -.
DR   Proteomes; UP000199578; 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; 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; SIGNAL PEPTIDASE I; 1.
DR   PANTHER; PTHR43390:SF8; 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   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003993};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199578}.
FT   DOMAIN          9..174
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        80
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   185 AA;  21461 MW;  BDF8CDC4214C1B13 CRC64;
     MTKKKNEVWE WTKALVIAVL LAAVIRYFLF APIVVDGLSM MPTLHDQDRM IVNKFGYTIG
     EPKRFDIIVF HAPENKDYIK RIIGLPGDRI EYKDDTLYVN GKAYEEPYLD EYKKKVIDGP
     LTDPFTLIEK TGKETVPEGH LFVMGDNRRN SKDSRHIGTI PMEKVLGNTS FVYWPFEDIR
     SVKMK
//
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