(data stored in ACNUC7421 zone)

SWISSPROT: B4SR39_STRM5

ID   B4SR39_STRM5            Unreviewed;       330 AA.
AC   B4SR39;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 52.
DE   SubName: Full=Patatin {ECO:0000313|EMBL:ACF49740.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0035 {ECO:0000313|EMBL:ACF49740.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49740.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49740.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49740.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01161}.
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DR   EMBL; CP001111; ACF49740.1; -; Genomic_DNA.
DR   RefSeq; WP_012509619.1; NC_011071.1.
DR   STRING; 391008.Smal_0035; -.
DR   EnsemblBacteria; ACF49740; ACF49740; Smal_0035.
DR   KEGG; smt:Smal_0035; -.
DR   eggNOG; ENOG4105D78; Bacteria.
DR   eggNOG; COG1752; LUCA.
DR   HOGENOM; HOG000261884; -.
DR   KO; K07001; -.
DR   OMA; IMGQSIN; -.
DR   OrthoDB; 373926at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00175-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; SSF52151; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   4: Predicted;
DR   PRODOM; B4SR39.
DR   SWISS-2DPAGE; B4SR39.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid degradation {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Lipid metabolism {ECO:0000256|PROSITE-ProRule:PRU01161};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    330       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002823701.
FT   DOMAIN       47    205       PNPLA. {ECO:0000259|PROSITE:PS51635}.
FT   MOTIF        78     82       GXSXG. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01161}.
FT   MOTIF       192    194       DGA/G. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01161}.
FT   ACT_SITE     80     80       Nucleophile. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01161}.
FT   ACT_SITE    192    192       Proton acceptor. {ECO:0000256|PROSITE-
FT                                ProRule:PRU01161}.
SQ   SEQUENCE   330 AA;  34141 MW;  8FE7DD456764677E CRC64;
     MSLFRPRMLL SVALVGLLAG CGGDPVRPTP PPAPTVVPQA KPVKIGIALG GGAAKGFAHI
     GVIKMLEANG FEPAVVSGTS AGSVVGALYA SGMDAFQMQS KAVALDEASI RDVRLFSGGL
     VQGQKLQDYV NEQVANRSAE RLKKPFAAVA TQLETGERAI FVRGNVGQAV RASSSIPGVF
     EPVKIGGRNY IDGGVVSPVP VDAARQLGAD FVIAVDISSK ASGKAPTDML GIVNQSISIM
     GQRLGEQELA RADIVIRPKV LDIGAADFSQ RGTAILEGEK AAMAAMPQIR AKIQQLQRAR
     AAAAAPAPVA APKCEEASRL GKLMGRKDKC
//

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