ID B8DVT2_BIFA0 Unreviewed; 241 AA.
AC B8DVT2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 Name=lepB {ECO:0000313|EMBL:ACL28583.1};
GN OrderedLocusNames=BLA_0281 {ECO:0000313|EMBL:ACL28583.1};
OS Bifidobacterium animalis subsp. lactis (strain AD011).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL28583.1, ECO:0000313|Proteomes:UP000002456};
RN [1] {ECO:0000313|EMBL:ACL28583.1, ECO:0000313|Proteomes:UP000002456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD011 {ECO:0000313|EMBL:ACL28583.1,
RC ECO:0000313|Proteomes:UP000002456};
RX PubMed=19011029; DOI=10.1128/JB.01515-08;
RA Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT lactis AD011.";
RL J. Bacteriol. 191:678-679(2009).
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}.
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DR EMBL; CP001213; ACL28583.1; -; Genomic_DNA.
DR RefSeq; WP_004268409.1; NC_011835.1.
DR AlphaFoldDB; B8DVT2; -.
DR STRING; 442563.BLA_0281; -.
DR MEROPS; S26.025; -.
DR GeneID; 66532658; -.
DR KEGG; bla:BLA_0281; -.
DR PATRIC; fig|442563.4.peg.299; -.
DR HOGENOM; CLU_028723_0_1_11; -.
DR Proteomes; UP000002456; Chromosome.
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:ACL28583.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000002456};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 48..72
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 46..219
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 76
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 128
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 241 AA; 26359 MW; B7EE304B23AD17C3 CRC64;
MDSSNEPMPQ SPAPMETHGN RDAGAGNLDS AGTEQQLAST RGTAIRDFFL WCAIPVAIVV
LLRIFVFGMY VIPSRSMENT IMPGDRVITT KLSPRPVALK RGDIVVFKDP SNWLASEETT
YHSDYLIKRL IGMPGDTVEC EGAGQPVKIN GVAIDESAYV KPGDQPSTFP FKVTVSEGHV
FVMGDNRSNS ADSRFHLNDA QHGQVPIRDI AGVAFARYWP LNRISWLSNY SDVFANVPDA
G
//
