ID A5GT33_SYNR3 Unreviewed; 190 AA.
AC A5GT33;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 88.
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:CAK28042.1};
GN OrderedLocusNames=SynRCC307_1139 {ECO:0000313|EMBL:CAK28042.1};
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK28042.1, ECO:0000313|Proteomes:UP000001115};
RN [1] {ECO:0000313|EMBL:CAK28042.1, ECO:0000313|Proteomes:UP000001115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RA Genoscope;
RL Submitted (MAY-2006) 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; CT978603; CAK28042.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GT33; -.
DR STRING; 316278.SynRCC307_1139; -.
DR MEROPS; S26.A02; -.
DR KEGG; syr:SynRCC307_1139; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_5_1_3; -.
DR OMA; IEPRWIP; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000001115; 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; IPR019757; Pept_S26A_signal_pept_1_Lys-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; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:CAK28042.1};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT DOMAIN 18..176
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 45
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 190 AA; 20812 MW; 2786FF73FD6927C9 CRC64;
MLADRPVMEQ RNTWRQQLQG LLLVVVVAIA LRWGVVEPRW IPSESMQPGL QPQDRILVWK
LGHRLGLSPG RNAVVVFRTP EVLAAAGYDP NAALIKRVVG VPGDAIAVES GTLQRNGLPV
SEPWIAEAMD YQLEPLTVEE GTLLVLGDNR NASLDSHLWG LLKEADVVGT ARWRYWPLAG
FGPISAPAMG
//