ID   AIS_ECOUT               Reviewed;         200 AA.
AC   Q1R9G3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   25-MAY-2022, entry version 76.
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=UTI89_C2534;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE08001.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000243; ABE08001.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000879110.1; NC_007946.1.
DR   AlphaFoldDB; Q1R9G3; -.
DR   SMR; Q1R9G3; -.
DR   EnsemblBacteria; ABE08001; ABE08001; UTI89_C2534.
DR   KEGG; eci:UTI89_C2534; -.
DR   HOGENOM; CLU_106705_1_0_6; -.
DR   OMA; NFTVIVW; -.
DR   UniPathway; UPA00451; -.
DR   Proteomes; UP000001952; 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_0000380559"
SQ   SEQUENCE   200 AA;  22394 MW;  898F0C82CD3AFB1D CRC64;
     MLAFCRSSLK SKKYFIILLA LAAIAGLGTH AAWSSNGLPR IDNKTLARLA QQHPVVVLFR
     HAERCDRSTN QCLSDKTGIT VKGTQDAREL GNAFSADIPD FDLYSSNTVR TIQSATWFSA
     GKKLTVDKRF LQCGNEIYSA IKDLQRKAPD KNIVIFTHNH CLTYIAKDKR DATFKPDYLD
     GLVMHVEKGK VYLDGEFVNH