ID A0A1C4LY79_9ACTN Unreviewed; 372 AA.
AC A0A1C4LY79;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=GA0115242_114545 {ECO:0000313|EMBL:SCD78702.1};
OS Streptomyces sp. SolWspMP-5a-2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1838281 {ECO:0000313|EMBL:SCD78702.1, ECO:0000313|Proteomes:UP000199131};
RN [1] {ECO:0000313|EMBL:SCD78702.1, ECO:0000313|Proteomes:UP000199131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SolWspMP-5a-2 {ECO:0000313|EMBL:SCD78702.1,
RC ECO:0000313|Proteomes:UP000199131};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; FMCI01000135; SCD78702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4LY79; -.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000199131; 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};
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 65..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 64..261
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 170
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 372 AA; 40509 MW; 01F7F09E1AE58D4E CRC64;
MGNRGRPRGE PNSPAENLLP TGLRRTGGGA GGGGGQSSAG RTRAERRRLQ RKVKRRRRRS
AVKEIPLLVG VAVLIALVLK TFLLQAFVIP SGSMEQTIQI GDRVLVDKLT PWFGSKPERG
DVVVFKDPGG WLQDEQSTVK KNDPIVVKQV KEGLTFIGLL PSEDEKDLIK RVVGVGGDRV
KCCDTQGRVT VNGVPLDEGA YLYPGNAPSL QAFDITVPQG RLWVMGDHRA NSADSRAHQD
TDYGGTVSED SVVGRARVIA WPFGHWNSLQ EPKTFSSVSN SVSGAAAAPR VSHRVASDDP
NGSIPLPSPA ELPLVMGVVG LHRVWGRRQR RVRSWRGGCG GWRTVRTRRR GAPRTSRGRS
GPGRGRRREL RE
//
