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Database: UniProt
Entry: D9W0T2_9ACTN
LinkDB: D9W0T2_9ACTN
Original site: D9W0T2_9ACTN 
ID   D9W0T2_9ACTN            Unreviewed;       252 AA.
AC   D9W0T2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE            EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN   ORFNames=SSNG_05160 {ECO:0000313|EMBL:EFL17908.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL17908.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL17908.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL17908.1,
RC   ECO:0000313|Proteomes:UP000005763};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. strain C.";
RL   Submitted (FEB-2009) 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|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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362042}.
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DR   EMBL; GG657750; EFL17908.1; -; Genomic_DNA.
DR   RefSeq; WP_007266834.1; NZ_GG657750.1.
DR   AlphaFoldDB; D9W0T2; -.
DR   STRING; 253839.SSNG_05160; -.
DR   eggNOG; COG0681; Bacteria.
DR   HOGENOM; CLU_028723_0_2_11; -.
DR   Proteomes; UP000005763; 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; 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.
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        21..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   TRANSMEM        213..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362042"
FT   DOMAIN          26..188
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        94
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   252 AA;  25895 MW;  B4DCAA795F64E252 CRC64;
     MGGTQAIRAR RDGRGGLGNT LSGIAVAIGF VLFLGGFVWG ALVYQPYTVP TDSMVPTVRP
     GDRVLAQRID GGQVRRGDVV VFTDTVWSNS PMVKRVVGVG GDTVSCCGQG GRVTVNGRAL
     DEPYVDREGD GAAAAGSTTF EVKVPEGNLF LMGDRRGGSL DSRAHLQDAG QGTVPRSAVS
     ARVDALAWPS AKMLERPQVF AALPGGTSAP GPLRLQVTAV LAGAGLVLLG GAYGPLARLL
     GRGRGRAGSD GR
//
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