LIP2_STAAN
ID LIP2_STAAN Reviewed; 691 AA.
AC Q7A7P2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Lipase 2;
DE EC=3.1.1.3;
DE AltName: Full=Glycerol ester hydrolase 2;
DE Flags: Precursor;
GN Name=lip2; Synonyms=geh; OrderedLocusNames=SA0309;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; BA000018; BAB41533.1; -; Genomic_DNA.
DR PIR; B89797; B89797.
DR RefSeq; WP_000943819.1; NC_002745.2.
DR AlphaFoldDB; Q7A7P2; -.
DR SMR; Q7A7P2; -.
DR ESTHER; staau-lipas; Bacterial_lip_FamI.6.
DR EnsemblBacteria; BAB41533; BAB41533; BAB41533.
DR KEGG; sau:SA0309; -.
DR HOGENOM; CLU_023555_2_0_9; -.
DR OMA; DNMVASI; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005877; YSIRK_signal_dom.
DR Pfam; PF04650; YSIRK_signal; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01168; YSIRK_signal; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT PROPEP 38..296
FT /evidence="ECO:0000250"
FT /id="PRO_0000045190"
FT CHAIN 297..691
FT /note="Lipase 2"
FT /id="PRO_0000045191"
FT REGION 34..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 604
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 646
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT BINDING 580
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 645
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
SQ SEQUENCE 691 AA; 76543 MW; 11F2117D26C54C7A CRC64;
MLRGQEERKY SIRKYSIGVV SVLAATMFVV SSHEAQASEK TPTSNAAAQK ETLNQPGEQG
NAITSHQMQS GKQLDDMHKE NGKSGTVTEG KDTLQSSKHQ STQNSKTIRT QNDNQVKQDS
ERQGSKQSHQ NNATNNTERQ NDQVQNTHHA ERNGSQSTTS QSNDVDKSQP SIPAQKVLPN
HDKAAPTSTT PPSNDKTAPK STKAQDATTD KHPNQQDTHQ PAHQIIDAKQ DDTVRQSEQK
PQVGDLSKHI DGQNSPEKPT DKNTDNKQLI KDALQAPKTR STTNAAADAK KVRPLKANQV
QPLNKYPVVF VHGFLGLVGD NAPALYPNYW GGNKFKVIEE LRKQGYNVHQ ASVSAFGSNY
DRAVELYYYI KGGRVDYGAA HAAKYGHERY GKTYKGIMPN WEPGKKVHLV GHSMGGQTIR
LMEEFLRNGN KEEIAYHKAH GGEISPLFTG GHNNMVASIT TLATPHNGSQ AADKFGNTEA
VRKIMFALNR FMGNKYSNID LGLTQWGFKQ LPNESYIDYI KRVSKSKIWT SDDNAAYDLT
LDGSAKLNNM TSMNPNITYT TYTGVSSHTG PLGYENPDLG TFFLMDTTSR IIGHDAREEW
RKNDGVVPVI SSLHPSNQPF INVTNDEPAT RRGIWQVKPI IQGWDHVDFI GVDFLDFKRK
GAELANFYTG IINDLLRVEA TESKGTQLKA S
