ID AIS_ECO81 Reviewed; 200 AA.
AC B7MXD4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=ECED1_2718;
OS Escherichia coli O81 (strain ED1a).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585397;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ED1a;
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; CU928162; CAR08750.1; -; Genomic_DNA.
DR RefSeq; WP_000879110.1; NC_011745.1.
DR AlphaFoldDB; B7MXD4; -.
DR SMR; B7MXD4; -.
DR KEGG; ecq:ECED1_2718; -.
DR HOGENOM; CLU_106705_1_0_6; -.
DR UniPathway; UPA00451; -.
DR Proteomes; UP000000748; 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 Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF011416; Ais-TraG-AfrS; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 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_0000380571"
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
//
