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Database: UniProt
Entry: D5ZX62_STRV1
LinkDB: D5ZX62_STRV1
Original site: D5ZX62_STRV1 
ID   D5ZX62_STRV1            Unreviewed;       167 AA.
AC   D5ZX62;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFE65172.2};
GN   ORFNames=SSFG_00426 {ECO:0000313|EMBL:EFE65172.2};
OS   Streptomyces viridosporus (strain ATCC 14672 / DSM 40746 / JCM 4963 / KCTC
OS   9882 / NRRL B-12104 / FH 1290) (Streptomyces ghanaensis).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=566461 {ECO:0000313|EMBL:EFE65172.2, ECO:0000313|Proteomes:UP000003824};
RN   [1] {ECO:0000313|Proteomes:UP000003824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14672 / DSM 40746 / JCM 4963 / KCTC 9882 / NRRL B-12104 /
RC   FH 1290 {ECO:0000313|Proteomes:UP000003824};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Ward D., Young S., Kodira C.D., Zeng Q., Koehrsen M.,
RA   Godfrey P., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland B.L.C., Ilzarbe M.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces ghanaensis ATCC 14672.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S26 family.
CC       {ECO:0000256|ARBA:ARBA00009370}.
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DR   EMBL; DS999641; EFE65172.2; -; Genomic_DNA.
DR   AlphaFoldDB; D5ZX62; -.
DR   eggNOG; COG0681; Bacteria.
DR   Proteomes; UP000003824; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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   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; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..167
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039637227"
FT   DOMAIN          9..102
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   DOMAIN          114..151
FT                   /note="Peptidase S26"
FT                   /evidence="ECO:0000259|Pfam:PF10502"
FT   ACT_SITE        33
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT   ACT_SITE        91
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ   SEQUENCE   167 AA;  17882 MW;  263DF4CE5FE28B2A CRC64;
     MSSALPALLV SAALALARAA ERRWVAASVS GGSMEPAYHD GDSVVVRRRA VPVRGAVVVV
     ERPPYRAPWP DAPVARTAPA HVLYARHWFI KRVAAVPGDP VPRAQVPALA DVPEDTVPEG
     MLVLLGDNRD DSYDSRSVGY FPESRVLGTV EGAGQPVPRS TARMRKT
//
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