ID D9VZX4_9ACTN Unreviewed; 518 AA.
AC D9VZX4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Protease {ECO:0000313|EMBL:EFL15734.1};
GN ORFNames=SSNG_02986 {ECO:0000313|EMBL:EFL15734.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15734.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL15734.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL15734.1,
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 -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; GG657750; EFL15734.1; -; Genomic_DNA.
DR RefSeq; WP_007264678.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VZX4; -.
DR STRING; 253839.SSNG_02986; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_013364_3_1_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:EFL15734.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..518
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038791245"
FT DOMAIN 118..286
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 414..514
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 348..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 54437 MW; 67728F7883D4E834 CRC64;
MPRPRPRLRT ATGTACAASA VVLAASLTAA PAAPAAPAAP AAPAITPTAT RAPIRWGDCP
LERVPAGMRC AEVTVPLDYA HPAKGTTRIA VARIPATAPG RRPLGSLLLN FGGPGGPGIA
SLAADPRPFA KLGERYDLVA FDPRGVGLST PVSCGGSQET GDEVPGDAAS QLAALRAVAE
RCALHSGPVL PYIGTVNVSR DMDRIRGALG DKKLNYLGFS YGTRLGAVYA AQFPRRTGRM
VLDGVDTLTE PLTEQALVSA RGQQRALENF LGWCAHQYDC VYGTNTRTAR EKVEALVERL
DEHPLVGDDG SHFTGQDAVG AIGAALYSRS LWPDLAEALA RVERDHDPVP LMELGGPDAS
PPTDGPTKVP DDNAAAALTA VNCADDPDRS NDKASPEAIE QEIRDLRDEF HRTSPVFGPG
QLMTVLSCYG RPAGTDFIRR IDHPGAPRML LVGTRGDPAT PYEWTEETAR RLGSAVVIDH
KGDGHTGYAT SACVRGYVDE FLIAGKLPGG TRSCPAGE
//
