ID   AIS_ECOLI               Reviewed;         200 AA.
AC   P45565; P77314;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   28-JAN-2026, entry version 149.
DE   RecName: Full=Lipopolysaccharide core heptose(II)-phosphate phosphatase;
DE            EC=3.1.3.-;
DE   AltName: Full=Polymyxin resistance protein PmrG;
DE   Flags: Precursor;
GN   Name=ais; Synonyms=pmrG; OrderedLocusNames=b2252, JW2246;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Guzzo A., Macintyre G., Diorio C., Salmon K., Dubow M.S.;
RT   "Identification, sequencing and characterization of an aluminium-inducible
RT   Escherichia coli gene.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   INDUCTION BY ZINC.
RX   PubMed=15659689; DOI=10.1128/jb.187.3.1124-1134.2005;
RA   Lee L.J., Barrett J.A., Poole R.K.;
RT   "Genome-wide transcriptional response of chemostat-cultured Escherichia
RT   coli to zinc.";
RL   J. Bacteriol. 187:1124-1134(2005).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of heptose(II) of the outer
CC       membrane lipopolysaccharide core. {ECO:0000250}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       metabolism.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- INDUCTION: Induced by BasR (By similarity). Expression is significantly
CC       induced in the presence of zinc. {ECO:0000250,
CC       ECO:0000269|PubMed:15659689}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. Ais
CC       subfamily. {ECO:0000305}.
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DR   EMBL; X83874; CAA58754.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75312.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16075.1; -; Genomic_DNA.
DR   PIR; B64996; B64996.
DR   RefSeq; NP_416755.1; NC_000913.3.
DR   RefSeq; WP_000879112.1; NZ_CP009789.1.
DR   AlphaFoldDB; P45565; -.
DR   SMR; P45565; -.
DR   BioGRID; 4260487; 13.
DR   FunCoup; P45565; 40.
DR   IntAct; P45565; 2.
DR   STRING; 511145.b2252; -.
DR   PaxDb; 511145-b2252; -.
DR   EnsemblBacteria; AAC75312; AAC75312; b2252.
DR   GeneID; 944945; -.
DR   KEGG; ecj:JW2246; -.
DR   KEGG; eco:b2252; -.
DR   KEGG; ecoc:C3026_12580; -.
DR   PATRIC; fig|511145.12.peg.2344; -.
DR   EchoBASE; EB2949; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_106705_1_0_6; -.
DR   InParanoid; P45565; -.
DR   OMA; NFTVIVW; -.
DR   OrthoDB; 6195868at2; -.
DR   PhylomeDB; P45565; -.
DR   BioCyc; EcoCyc:G7165-MONOMER; -.
DR   UniPathway; UPA00451; -.
DR   PRO; PR:P45565; -.
DR   Proteomes; UP000000625; 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   CDD; cd07040; HP; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 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   NCBIfam; NF011945; PRK15416.1; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   PIRSF; PIRSF011416; Ais-TraG-AfrS; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..200
FT                   /note="Lipopolysaccharide core heptose(II)-phosphate
FT                   phosphatase"
FT                   /id="PRO_0000064515"
FT   CONFLICT        200
FT                   /note="H -> Y (in Ref. 1; CAA58754)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   200 AA;  22257 MW;  A210382654AC6B35 CRC64;
     MLAFCRSSLK SKKYIIILLA LAAIAGLGTH AAWSSNGLPR IDNKTLARLA QQHPVVVLFR
     HAERCDRSTN QCLSDKTGIT VKGTQDAREL GNAFSADIPD FDLYSSNTVR TIQSATWFSA
     GKKLTVDKRL LQCGNEIYSA IKDLQSKAPD KNIVIFTHNH CLTYIAKDKR DATFKPDYLD
     GLVMHVEKGK VYLDGEFVNH
//