ID   AIS_SALPB               Reviewed;         201 AA.
AC   A9N5B6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 63.
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=SPAB_00686;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX66112.1; -; Genomic_DNA.
DR   RefSeq; WP_000879248.1; NC_010102.1.
DR   AlphaFoldDB; A9N5B6; -.
DR   SMR; A9N5B6; -.
DR   KEGG; spq:SPAB_00686; -.
DR   PATRIC; fig|1016998.12.peg.646; -.
DR   HOGENOM; CLU_106705_1_0_6; -.
DR   OMA; NFTVIVW; -.
DR   BioCyc; SENT1016998:SPAB_RS02855-MON; -.
DR   UniPathway; UPA00451; -.
DR   Proteomes; UP000008556; 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_0000380582"
SQ   SEQUENCE   201 AA;  22027 MW;  A34132FD78210504 CRC64;
     MLAFTLRFIK NKRYFAILAG ALVIIAGLTS QHAWSGNGLP QINGKALAAL AKQHPVVVLF
     RHAERCDRSD NTCLSDSTGI TVKGAQDARA LGKAFSADIQ NYNLYSSNTV RTIQSATWFS
     AGRSLTVDKK MMDCGSGIYA SINTLLKKSQ NKNIVIFTHN HCLTYIAKNK RGVKFDPDYL
     NALVMHAENG KLFLDGEFVP G