ID A0A087BR60_9BIFI Unreviewed; 273 AA.
AC A0A087BR60;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN ORFNames=BMIN_0940 {ECO:0000313|EMBL:KFI73510.1};
OS Bifidobacterium minimum.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1693 {ECO:0000313|EMBL:KFI73510.1, ECO:0000313|Proteomes:UP000029014};
RN [1] {ECO:0000313|EMBL:KFI73510.1, ECO:0000313|Proteomes:UP000029014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 11592 {ECO:0000313|EMBL:KFI73510.1,
RC ECO:0000313|Proteomes:UP000029014};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) 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:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC pass type II membrane protein {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:KFI73510.1}.
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DR EMBL; JGZD01000006; KFI73510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087BR60; -.
DR STRING; 1693.BMIN_0940; -.
DR eggNOG; COG0681; Bacteria.
DR Proteomes; UP000029014; Unassembled WGS sequence.
DR GO; GO:0016020; C: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; 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; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:KFI73510.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000029014};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 74..249
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 273 AA; 29276 MW; FA8455D82A5F7EA4 CRC64;
MSDSVSSRIP TQDAAEDSHI LEVADHGVDP RPLSTFSGSS VGAASHSMHT PSGRSPRPRR
RRGRHIDRSR FRLRDVVVYC GIPILVVVLV RVFVIGLYVI PSGSMMDTIE IGDRVVTSRL
SARPSSLRRG DVVVFRDPAH WLSDETTSSS LGGNYLIKRL IGLPGDLVAC KGGGSPVTIN
GVAVDESSYI RPGVEPSSFS FSVKVTAGHV FVMGDNRANS ADSRYHQNDG DDGLVPMSDI
VGVGVAIYWP ISRMSGLDSH HEVFADVPNG TVG
//
