ID A0A0W0TI44_9GAMM Unreviewed; 341 AA.
AC A0A0W0TI44;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Acid phosphatase {ECO:0000313|EMBL:KTC95254.1, ECO:0000313|EMBL:SPX59701.1};
DE EC=3.1.3.2 {ECO:0000313|EMBL:SPX59701.1};
GN Name=map_2 {ECO:0000313|EMBL:KTC95254.1};
GN ORFNames=Lfee_2918 {ECO:0000313|EMBL:KTC95254.1}, NCTC12022_00412
GN {ECO:0000313|EMBL:SPX59701.1};
OS Legionella feeleii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=453 {ECO:0000313|EMBL:KTC95254.1, ECO:0000313|Proteomes:UP000054698};
RN [1] {ECO:0000313|EMBL:KTC95254.1, ECO:0000313|Proteomes:UP000054698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-44C {ECO:0000313|EMBL:KTC95254.1,
RC ECO:0000313|Proteomes:UP000054698};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SPX59701.1, ECO:0000313|Proteomes:UP000251942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12022 {ECO:0000313|EMBL:SPX59701.1,
RC ECO:0000313|Proteomes:UP000251942};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000256|ARBA:ARBA00005375}.
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DR EMBL; LNYB01000085; KTC95254.1; -; Genomic_DNA.
DR EMBL; UASS01000002; SPX59701.1; -; Genomic_DNA.
DR RefSeq; WP_058447724.1; NZ_UASS01000002.1.
DR AlphaFoldDB; A0A0W0TI44; -.
DR STRING; 453.Lfee_2918; -.
DR PATRIC; fig|453.4.peg.3189; -.
DR OrthoDB; 5605418at2; -.
DR Proteomes; UP000054698; Unassembled WGS sequence.
DR Proteomes; UP000251942; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd07061; HP_HAP_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR000560; His_Pase_clade-2.
DR InterPro; IPR029033; His_PPase_superfam.
DR PANTHER; PTHR11567:SF110; ACID PHOSPHATASE 1, ISOFORM B; 1.
DR PANTHER; PTHR11567; ACID PHOSPHATASE-RELATED; 1.
DR Pfam; PF00328; His_Phos_2; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:SPX59701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054698};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..341
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036003010"
SQ SEQUENCE 341 AA; 39023 MW; E7083EF5AF5FE1E8 CRC64;
MKVLIKNCFF IFLAVAVSNA FAQEKLIFAL ELIRHGDRTP LEEIPNAPHD WKRGVGELTQ
RGWYQELESG RAARKKYVKQ YHLLPANYNP RLVYVRSTDT KRTIASANAF LLGLYPSKMR
RGSIPVHAIS KSQDNLLIVT PGKNIFSLIK LYFISRKAWQ EQTSYRQEKL RRWRSITGLS
LKNYQQIVPL ADNLYIRRIH HVPMPKGISN DDANEIIQLG KWAVVNYFKL RQVSYPMGHS
FLNETNNYFV NAVEKRSSLK YVLLSAHDSS IMSVMATLGA PLESIPPYAS HVDFALFKNN
KNYYIRVSYN DKLVTIPACG GTVCSLSQFY VLAQATKQQI A
//
