(data stored in SCRATCH zone)

SWISSPROT: B4SR42_STRM5

ID   B4SR42_STRM5            Unreviewed;       279 AA.
AC   B4SR42;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 61.
DE   RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE            EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0038 {ECO:0000313|EMBL:ACF49743.1};
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:ACF49743.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49743.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49743.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC         Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000897};
CC   -!- SIMILARITY: Belongs to the class A bacterial acid phosphatase
CC       family. {ECO:0000256|PIRNR:PIRNR000897}.
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DR   EMBL; CP001111; ACF49743.1; -; Genomic_DNA.
DR   RefSeq; WP_004133277.1; NC_011071.1.
DR   STRING; 391008.Smal_0038; -.
DR   EnsemblBacteria; ACF49743; ACF49743; Smal_0038.
DR   KEGG; smt:Smal_0038; -.
DR   eggNOG; ENOG4105SBG; Bacteria.
DR   eggNOG; COG0671; LUCA.
DR   HOGENOM; HOG000233901; -.
DR   KO; K09474; -.
DR   OMA; MGQSRVI; -.
DR   OrthoDB; 1930882at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00190-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd03397; PAP2_acid_phosphatase; 1.
DR   InterPro; IPR001011; Acid_Pase_classA_bac.
DR   InterPro; IPR018296; Acid_Pase_classA_bac_CS.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Pfam; PF01569; PAP2; 1.
DR   PIRSF; PIRSF000897; Acid_Ptase_ClsA; 1.
DR   PRINTS; PR00483; BACPHPHTASE.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; SSF48317; 1.
DR   PROSITE; PS01157; ACID_PHOSPH_CL_A; 1.
PE   3: Inferred from homology;
DR   PRODOM; B4SR42.
DR   SWISS-2DPAGE; B4SR42.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR000897,
KW   ECO:0000313|EMBL:ACF49743.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     21       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        22    279       Acid phosphatase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002826286.
FT   DOMAIN      120    234       acidPPc. {ECO:0000259|SMART:SM00014}.
SQ   SEQUENCE   279 AA;  29404 MW;  A4484E314049A951 CRC64;
     MSLISHPARP LLGLAVVAAL AGCAATAAKP TAVEANITTK AVGYLDKSAV PGSLDLVPAP
     PVAGSAALAL DEQVSREARA LRGSPRFAQA GVDAELGFPE GANHFSCAAD IDVDAVKTPA
     LYRLLERSRI DASAATKAAK NHYQRPRPFM VNGEPTCAPK DEEGLRKNGS YPSGHTSIGW
     AWALILSEIA PDRADAIQAR GRNYGESRLV CNVHWQSDIL EGRFMGAAAV ARLHDNAAFN
     KDLLAARKEI AAARKAGLHS SRDCTTENAV LKVRPQSAL
//

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