ID A0A1G9KU41_9BACT Unreviewed; 380 AA.
AC A0A1G9KU41;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN04488090_1132 {ECO:0000313|EMBL:SDL52993.1};
OS Siphonobacter aquaeclarae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=563176 {ECO:0000313|EMBL:SDL52993.1, ECO:0000313|Proteomes:UP000198901};
RN [1] {ECO:0000313|EMBL:SDL52993.1, ECO:0000313|Proteomes:UP000198901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21668 {ECO:0000313|EMBL:SDL52993.1,
RC ECO:0000313|Proteomes:UP000198901};
RA de Groot N.N.;
RL Submitted (OCT-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; FNGS01000002; SDL52993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9KU41; -.
DR STRING; 563176.SAMN04488090_1132; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000198901; 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; 2.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 2.
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; 2.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 2.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 2.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000198901}.
FT DOMAIN 13..168
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT DOMAIN 310..357
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 43
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 380 AA; 43699 MW; 8B17DC24A52D6666 CRC64;
MFSRKKTRRS PVREWFHSLA FAVVAATLIR FLTLEAFAIP TPSMEHSLMV GDFLFVSKLH
YGIRTPQTPL QVPLTHQKIW GTNIPSYTDL IQLPTYRLPG FTHVRSGDVV VFNFPPPKPG
EPDYPMDLRT YLIKRCIGTP GDVVEIRREH VFVNGKEMAP PAGAQTSYLL RTTEELDDRF
FRKYGIVNDF ASKEGPFINW QPVEEQDSTG AVHKIGYQIL TTREVADDLK SQDWVQRLEP
MTEEPGRAEP GIYGTPAYAW NRDNFGPLLV PKKGMTIPVN ARTMAVYGPV IRRYEHQKDV
EVSGNRLKIN GKDLVSYTFT QDYYFMMGDN RHNSDDSRYW GFVPEDHVVG KAVFVWMSLD
PVPGDSWHTV RWSRLFRPIR
//
