ID A0A078LVG6_9STAP Unreviewed; 176 AA.
AC A0A078LVG6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU003993};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU003993};
GN Name=spsB {ECO:0000313|EMBL:CDZ99168.1};
GN ORFNames=BN1048_00293 {ECO:0000313|EMBL:CDZ99168.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CDZ99168.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CDZ99168.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CDZ99168.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Essential for cell viability.
CC {ECO:0000256|ARBA:ARBA00002312}.
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}.
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DR EMBL; CCSE01000001; CDZ99168.1; -; Genomic_DNA.
DR RefSeq; WP_035807650.1; NZ_CCSE01000001.1.
DR AlphaFoldDB; A0A078LVG6; -.
DR STRING; 1461582.BN1048_00293; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_0_9; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000044136; 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: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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU003993};
KW Membrane {ECO:0000256|RuleBase:RU003993};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003993};
KW Reference proteome {ECO:0000313|Proteomes:UP000044136};
KW Transmembrane {ECO:0000256|RuleBase:RU003993};
KW Transmembrane helix {ECO:0000256|RuleBase:RU003993}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU003993"
FT DOMAIN 5..167
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 36
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 176 AA; 19812 MW; 763F4D7771177F9F CRC64;
MAKEIREWAV AIFIAIVVIA VIRMFLFVTF AVDGLSMDPT LEDGDRVVVN KFIYDIGEVE
QDDVVVFESG QDSAYVKRII GVPGDTVEMK DKTVYLNGEP LQEDYVTHRG ESYMDNFTLS
DLGVEGEVIP EGHYLVLGDN RPISRDSRDF GLITEASIIG EVQLRFWPLN EIAIDF
//
