ID B2FLX5_STRMK Unreviewed; 455 AA.
AC B2FLX5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Phosphoesterase {ECO:0000313|EMBL:CAQ45343.1};
GN OrderedLocusNames=Smlt1822 {ECO:0000313|EMBL:CAQ45343.1};
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373 {ECO:0000313|EMBL:CAQ45343.1, ECO:0000313|Proteomes:UP000008840};
RN [1] {ECO:0000313|EMBL:CAQ45343.1, ECO:0000313|Proteomes:UP000008840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a {ECO:0000313|EMBL:CAQ45343.1,
RC ECO:0000313|Proteomes:UP000008840};
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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DR EMBL; AM743169; CAQ45343.1; -; Genomic_DNA.
DR AlphaFoldDB; B2FLX5; -.
DR EnsemblBacteria; CAQ45343; CAQ45343; Smlt1822.
DR KEGG; sml:Smlt1822; -.
DR PATRIC; fig|522373.3.peg.1744; -.
DR eggNOG; COG1409; Bacteria.
DR eggNOG; COG3540; Bacteria.
DR HOGENOM; CLU_035600_0_0_6; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR039331; PPA-like.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR PANTHER; PTHR22953; ACID PHOSPHATASE RELATED; 1.
DR PANTHER; PTHR22953:SF153; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008840};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..455
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002775893"
FT DOMAIN 45..140
FT /note="Purple acid phosphatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16656"
FT DOMAIN 149..347
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT REGION 425..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 455 AA; 49840 MW; EDE354CF96CB84C9 CRC64;
MSGRCLMRTL ALGLLLAVPS LCFAAAEANT QVPAGSRHYA ATTVPDRIVA SPAGDPGHGF
AVAWRTDGSM QAPLLEIALA GDSPAIEGIR QVRATTRALQ TENGLSHHHR ADVSGLRPDT
LYVYRVQGNG SWSAWNQLRT LAAPDQPLTL LYFGDTQNKN VSHVSRVVRA AQKAAPEARL
SLFAGDLVSG GDGADDSEWG EWFAAAGWLA QETLVAPAIG NHEYVEEFED TPQERRVLGR
HWPVTFALPG NGASAAQQTS YWFDAQGVRV AVVDGTSALD LGTAKAQAQW LDKVLTGNPQ
PWTLVLLHQP FYSPREGREN GALRDVLLPV VRRHNVDLVL QGHDHTYGRR GEGQAATPQY
VVTVAGPKQY RLSDEARRTM DPVAEDTQLF QVLHIDPQHL RYEARTVTGR LYDAFELRRD
AKGGKQRTEL TEGRITPRDC PRAQTAKGRA DRCWE
//
