ID   AIS_ECOLU               Reviewed;         200 AA.
AC   B7N5L7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=ECUMN_2593;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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; CU928163; CAR13776.1; -; Genomic_DNA.
DR   RefSeq; WP_001306469.1; NC_011751.1.
DR   RefSeq; YP_002413304.1; NC_011751.1.
DR   AlphaFoldDB; B7N5L7; -.
DR   SMR; B7N5L7; -.
DR   STRING; 585056.ECUMN_2593; -.
DR   EnsemblBacteria; CAR13776; CAR13776; ECUMN_2593.
DR   KEGG; eum:ECUMN_2593; -.
DR   PATRIC; fig|585056.7.peg.2774; -.
DR   HOGENOM; CLU_106705_1_0_6; -.
DR   OMA; NFTVIVW; -.
DR   UniPathway; UPA00451; -.
DR   Proteomes; UP000007097; 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..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01868"
FT   CHAIN           26..200
FT                   /note="Lipopolysaccharide core heptose(II)-phosphate
FT                   phosphatase"
FT                   /id="PRO_0000380564"
SQ   SEQUENCE   200 AA;  22291 MW;  AB86A720CD3AF435 CRC64;
     MLAFCRSSLK SKKYFIILLA LAAIAGLGTH AAWSSNGLPR IDNKTLARLA QQHPVVVLFR
     HAERCDRSTN QCLSDKTGIT VKGTQDAREL GNAFSADIPD FDLYSSNTVR TIQSATWFSA
     GKKLTVDKRL LQCGNEIYSA IKDLQSKAPD KNIVIFTHNH CLTYIAKDKR DATFKPDYLD
     GLVMHVEKGK VYLDGEFVNH