ID   AIS_SALPA               Reviewed;         201 AA.
AC   Q5PC78;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=SPA0567;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV76569.1; -; Genomic_DNA.
DR   RefSeq; WP_000879256.1; NC_006511.1.
DR   AlphaFoldDB; Q5PC78; -.
DR   SMR; Q5PC78; -.
DR   EnsemblBacteria; AAV76569; AAV76569; SPA0567.
DR   KEGG; spt:SPA0567; -.
DR   HOGENOM; CLU_106705_1_0_6; -.
DR   OMA; NFTVIVW; -.
DR   UniPathway; UPA00451; -.
DR   Proteomes; UP000008185; 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_0000380580"
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