ID A0A2S9BTQ0_9MICO Unreviewed; 240 AA.
AC A0A2S9BTQ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:PRB65086.1};
GN ORFNames=CQ034_02880 {ECO:0000313|EMBL:PRB65086.1};
OS Microbacterium sp. MYb45.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1827294 {ECO:0000313|EMBL:PRB65086.1, ECO:0000313|Proteomes:UP000238044};
RN [1] {ECO:0000313|EMBL:PRB65086.1, ECO:0000313|Proteomes:UP000238044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MYb45 {ECO:0000313|EMBL:PRB65086.1,
RC ECO:0000313|Proteomes:UP000238044};
RA Zimmermann J., Obeng N., Yang W., Obeng O., Kissoyan K., Pees B.,
RA Dirksen P., Hoppner M., Franke A., Rosenstiel P., Leippe M., Dierking K.,
RA Kaleta C., Schulenburg H.;
RT "Genomic, metabolic, and phenotypic characteristics of bacterial isolates
RT from the natural microbiome of the model nematode Caenorhabditis elegans.";
RL Submitted (SEP-2017) 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|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:PRB65086.1}.
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DR EMBL; PCPG01000001; PRB65086.1; -; Genomic_DNA.
DR RefSeq; WP_029263505.1; NZ_PCPG01000001.1.
DR AlphaFoldDB; A0A2S9BTQ0; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000238044; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 20..218
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 50
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 240 AA; 26409 MW; 0C4B46F86D91A03C CRC64;
MTDSPAARTS RRRGFLVFLR DVLVIIVIAA LVSFVVKSFV VRSFYIPSAS MERTLLVKDR
ILVDELTPRW TDYARGDVVV FKDPGGWLDP QPQTPAQPPL VQAVDWVLNF VGISATDSQD
HLVKRVIGLP GDHVVCCNAL GQITINGAPI DELSYLNLPE GDTAASNEPF DVVVPDDSVW
LLGDNRDRSR DARAHQDLPS GGFVPMENIV GKAFLTTWPL DRMGPIDGHH DTFNGVPDPE
//
