ID W9GCG0_9MICO Unreviewed; 237 AA.
AC W9GCG0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=N865_10235 {ECO:0000313|EMBL:EWT01514.1};
OS Intrasporangium oryzae NRRL B-24470.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Intrasporangium.
OX NCBI_TaxID=1386089 {ECO:0000313|EMBL:EWT01514.1, ECO:0000313|Proteomes:UP000019489};
RN [1] {ECO:0000313|EMBL:EWT01514.1, ECO:0000313|Proteomes:UP000019489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24470 {ECO:0000313|EMBL:EWT01514.1,
RC ECO:0000313|Proteomes:UP000019489};
RA Liu H., Wang G.;
RT "Intrasporangium oryzae NRRL B-24470.";
RL Submitted (AUG-2013) 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:EWT01514.1}.
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DR EMBL; AWSA01000021; EWT01514.1; -; Genomic_DNA.
DR RefSeq; WP_051510484.1; NZ_AWSA01000021.1.
DR AlphaFoldDB; W9GCG0; -.
DR STRING; 1386089.N865_10235; -.
DR PATRIC; fig|1386089.3.peg.2264; -.
DR eggNOG; COG0681; Bacteria.
DR OrthoDB; 9815782at2; -.
DR Proteomes; UP000019489; 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 Reference proteome {ECO:0000313|Proteomes:UP000019489};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 31..55
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 29..216
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 237 AA; 24968 MW; FACBA468C0413771 CRC64;
MTVEPAQEPG PTAPSSVPEA TRTRSARSLR WLVAPAVVLL AVLLVRAFLV TPFGIPSGSM
EDTLQVGDRV LVSRLTGPDE LRRGDVVVFD ASRAWGVGEP ASGPFQALVG AAQSLVGQGP
DTDYVKRVIG LPGDHVRCCT TNGRLEINGV AVDEPYLKAG DAPSLTTFDV TLPPDRFWVM
GDHRSASADS RAHLGGPGGG AVPGDDMIGK VWVRYWPLDR LGSLPTGPLS SVPRNGE
//