AIS_SALPK
ID AIS_SALPK Reviewed; 201 AA.
AC B5BCP9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Lipopolysaccharide core heptose(II)-phosphate phosphatase {ECO:0000255|HAMAP-Rule:MF_01868};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01868};
DE Flags: Precursor;
GN Name=ais {ECO:0000255|HAMAP-Rule:MF_01868}; OrderedLocusNames=SSPA0531;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
CC -!- FUNCTION: Catalyzes the dephosphorylation of heptose(II) of the outer
CC membrane lipopolysaccharide core. {ECO:0000255|HAMAP-Rule:MF_01868}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC metabolism. {ECO:0000255|HAMAP-Rule:MF_01868}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01868}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. Ais
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01868}.
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DR EMBL; FM200053; CAR58660.1; -; Genomic_DNA.
DR RefSeq; WP_000879256.1; NC_011147.1.
DR AlphaFoldDB; B5BCP9; -.
DR SMR; B5BCP9; -.
DR KEGG; sek:SSPA0531; -.
DR HOGENOM; CLU_106705_1_0_6; -.
DR OMA; NFTVIVW; -.
DR UniPathway; UPA00451; -.
DR Proteomes; UP000001869; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008653; P:lipopolysaccharide metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01868; Ais; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR011310; LipoPS_heptP_Pase.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF011416; Ais-TraG-AfrS; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01868"
FT CHAIN 36..201
FT /note="Lipopolysaccharide core heptose(II)-phosphate
FT phosphatase"
FT /id="PRO_0000380581"
SQ SEQUENCE 201 AA; 22001 MW; 1AAFBAF68D884020 CRC64;
MLAFTLRFIK NKRYLATLAG ALVIIAGLTS QHAWSGNGLP QINGKALAAL AKQHPVVVLF
RHAERCDRSD NTCLSDSTGI TVNGAQDARA LGKAFSADIQ NYNLYSSNTV RTIQSATWFS
AGRSFTVDKK MMDCGSGIYA SINTLLKKSQ NKNIVIFTHN HCLTYIAKNK RGVKFDPDYL
NALVMHAENG KLFLDGEFVP G