ID U2ZVZ7_9SPHN Unreviewed; 262 AA.
AC U2ZVZ7;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Acid phosphatase {ECO:0000256|PIRNR:PIRNR000897};
DE EC=3.1.3.2 {ECO:0000256|PIRNR:PIRNR000897};
GN ORFNames=NT2_05_04700 {ECO:0000313|EMBL:GAD49549.1};
OS Caenibius tardaugens NBRC 16725.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Caenibius.
OX NCBI_TaxID=1219035 {ECO:0000313|EMBL:GAD49549.1, ECO:0000313|Proteomes:UP000016568};
RN [1] {ECO:0000313|EMBL:GAD49549.1, ECO:0000313|Proteomes:UP000016568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16725 {ECO:0000313|EMBL:GAD49549.1,
RC ECO:0000313|Proteomes:UP000016568};
RA Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Novosphingobium tardaugens NBRC 16725.";
RL Submitted (SEP-2013) 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 family.
CC {ECO:0000256|PIRNR:PIRNR000897}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAD49549.1}.
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DR EMBL; BASZ01000005; GAD49549.1; -; Genomic_DNA.
DR RefSeq; WP_021690455.1; NZ_CP034179.1.
DR AlphaFoldDB; U2ZVZ7; -.
DR KEGG; ntd:EGO55_13610; -.
DR eggNOG; COG0671; Bacteria.
DR OrthoDB; 9805301at2; -.
DR Proteomes; UP000016568; Unassembled WGS sequence.
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 Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR001011; Acid_Pase_classA_bac.
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; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000897};
KW Reference proteome {ECO:0000313|Proteomes:UP000016568};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..262
FT /note="Acid phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030177824"
FT DOMAIN 115..225
FT /note="Phosphatidic acid phosphatase type 2/haloperoxidase"
FT /evidence="ECO:0000259|SMART:SM00014"
FT REGION 50..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 27525 MW; B589061009556577 CRC64;
MKHLWAVGLL ALAGAAVWAE QPLPTPETFR IPPGYLEQAD LPDSAALIPA PPVSGSAAQA
RDDAASRNGQ ALHGSARWDL ATADAELFSP HDTEALSCAA GFAIGPDSAP ATNRLLTRAM
IDLALSTSGA KKKYQRARPF MENGAPNCTP AHEAYLRKDG SYPSGHSAIG YGWGLIMAEL
VPARATELVA RGRAFGDSRR VCNVHWLSDI EEGRVVASAT VAKLHAAASF QKDLQAARDE
IAAGKLVAPK RDCAKEAAAL AL
//
