ID D3PZ28_STANL Unreviewed; 266 AA.
AC D3PZ28;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Triacylglycerol lipase {ECO:0000313|EMBL:ADD45457.1};
DE EC=3.1.1.3 {ECO:0000313|EMBL:ADD45457.1};
GN OrderedLocusNames=Snas_5827 {ECO:0000313|EMBL:ADD45457.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD45457.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD45457.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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DR EMBL; CP001778; ADD45457.1; -; Genomic_DNA.
DR RefSeq; WP_013021028.1; NC_013947.1.
DR AlphaFoldDB; D3PZ28; -.
DR STRING; 446470.Snas_5827; -.
DR KEGG; sna:Snas_5827; -.
DR eggNOG; COG2755; Bacteria.
DR HOGENOM; CLU_038449_3_0_11; -.
DR Proteomes; UP000000844; Chromosome.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR CDD; cd01823; SEST_like; 1.
DR Gene3D; 3.40.50.1110; SGNH hydrolase; 1.
DR InterPro; IPR037460; SEST-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR37981; LIPASE 2; 1.
DR PANTHER; PTHR37981:SF1; SGNH_HYDRO DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
DR SUPFAM; SSF52266; SGNH hydrolase; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637460-2};
KW Hydrolase {ECO:0000313|EMBL:ADD45457.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000844};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..266
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003048114"
FT DOMAIN 45..258
FT /note="SGNH hydrolase-type esterase"
FT /evidence="ECO:0000259|Pfam:PF13472"
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR637460-1"
FT ACT_SITE 252
FT /evidence="ECO:0000256|PIRSR:PIRSR637460-1"
FT DISULFID 64..88
FT /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
FT DISULFID 128..136
FT /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
FT DISULFID 185..234
FT /evidence="ECO:0000256|PIRSR:PIRSR637460-2"
SQ SEQUENCE 266 AA; 27636 MW; 614D8BB9330F2D86 CRC64;
MSSKSSPSRR LIARLSALAL TAAVALGTTL VASPATAAPL VFAGLGDSYA SGVGAGDYIG
SDDCYRSSHA YPKQVADAYG EYLYFNACSG AKVQDVIDNQ IGNISIAEHI TIGVGGNDAG
FSRVLGACAG TDTALCLSQV EAANTFIRDE LPARLDTLYT KVGERTTYAD VAVVGNPRLF
NGTTCAGTLA ITPEEQEALN GTADLLATTT KGVAADHGYR FVDPRDAFAS HAICSADPWL
LGWTGSQLES FHPNVAGQNA YTDLLL
//
