ID L7LN01_9ACTN Unreviewed; 288 AA.
AC L7LN01;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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:GAC62495.1};
GN ORFNames=GSI01S_35_00520 {ECO:0000313|EMBL:GAC62495.1};
OS Gordonia sihwensis NBRC 108236.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223544 {ECO:0000313|EMBL:GAC62495.1, ECO:0000313|Proteomes:UP000035083};
RN [1] {ECO:0000313|EMBL:GAC62495.1, ECO:0000313|Proteomes:UP000035083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108236 {ECO:0000313|EMBL:GAC62495.1,
RC ECO:0000313|Proteomes:UP000035083};
RA Yoshida I., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia sihwensis NBRC 108236.";
RL Submitted (DEC-2012) 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:GAC62495.1}.
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DR EMBL; BANU01000035; GAC62495.1; -; Genomic_DNA.
DR RefSeq; WP_006897905.1; NZ_BANU01000035.1.
DR AlphaFoldDB; L7LN01; -.
DR eggNOG; COG0681; Bacteria.
DR Proteomes; UP000035083; 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; 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; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000035083};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 59..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 57..272
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 166
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 288 AA; 31645 MW; FA7B0595737CBA02 CRC64;
MTDISTLFYV DDNTRGDDPS QANDERGSSG GAESDSGFTF RDDAPEDEQK GKSRWLRELL
IIVGIVLVLM FVFTQFFFRQ YVVPSESMEP TLHGCYGCTN DHIVVDKMVY RFSDPKPGDV
VVFKAPTSSW DEGWSSPRSS NPVVHKIQDV LSLFALAPPD ENNLVKRVIA VGGQTVQCRE
ADGKGVTVDG KPLHEPYIDK QLQAQTYQQS GGVLGQGSCY GSDFGPIKVP EGNLWVMGDN
RSNSADSRAH IDDEFHGTVP VSDVRGKVRF IIYPFSRIGG VGSVDPQS
//
