ID A0A291QG76_9ACTN Unreviewed; 227 AA.
AC A0A291QG76;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=KY5_5782 {ECO:0000313|EMBL:ATL30800.1};
OS Streptomyces formicae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL30800.1, ECO:0000313|Proteomes:UP000221011};
RN [1] {ECO:0000313|EMBL:ATL30800.1, ECO:0000313|Proteomes:UP000221011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY5 {ECO:0000313|EMBL:ATL30800.1,
RC ECO:0000313|Proteomes:UP000221011};
RA Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT producer.";
RL Submitted (AUG-2017) 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; CP022685; ATL30800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291QG76; -.
DR KEGG; sfk:KY5_5782; -.
DR Proteomes; UP000221011; 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; 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, ECO:0000313|EMBL:ATL30800.1};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000221011}.
FT DOMAIN 1..164
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
SQ SEQUENCE 227 AA; 24209 MW; F4297DE36335A2C2 CRC64;
MQNTLQQGDR VLVDKLTPWF GSEPERGEVV VFRDPGHWLD GEPTPDPNAI QRVLGWVGLM
PSADEKDLIK RVIGVGGDTV ECKGTGPVKV NGKALNEPYV FAGNTPCSVD DQGGQFKVTV
PKGKIWVMGD HRQNSLDSRY HQNQPGGGAV PVDNVVGRAI VIAWPPTRWA TLPKPDTFDQ
PGINALSSAA PGVLGLAGAV PIVLWRRRRL TVAAAQGARV SGGGTAR
//
