AIS_SALAR
ID AIS_SALAR Reviewed; 201 AA.
AC A9MJC7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=SARI_00601;
OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=41514;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980;
RG The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; CP000880; ABX20527.1; -; Genomic_DNA.
DR RefSeq; WP_000879144.1; NC_010067.1.
DR AlphaFoldDB; A9MJC7; -.
DR SMR; A9MJC7; -.
DR STRING; 41514.SARI_00601; -.
DR EnsemblBacteria; ABX20527; ABX20527; SARI_00601.
DR KEGG; ses:SARI_00601; -.
DR HOGENOM; CLU_106705_1_0_6; -.
DR OMA; NFTVIVW; -.
DR OrthoDB; 1642854at2; -.
DR UniPathway; UPA00451; -.
DR Proteomes; UP000002084; 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; IPR029033; His_PPase_superfam.
DR InterPro; IPR011310; LipoPS_heptP_Pase.
DR PIRSF; PIRSF011416; Ais-TraG-AfrS; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 3: Inferred from homology;
KW Hydrolase; Periplasm; Reference proteome; 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_0000380575"
SQ SEQUENCE 201 AA; 22086 MW; B3AC78204420DB2E CRC64;
MLAFILRFIK NKSYFALLAG AWVIIAGLTS QHAWSGNGLP QINGNTLAAL AKQYPVVVLF
RHAERCDRSD NTCLSDSSGI TVNGAQNARS LGKDFNADIQ NYNLYSSNTV RTIQSATWFS
AGRSLTVDKK MMDCGSGIYA SINTLLKKSQ NKNVVIFTHN HCLTYIAKNK RGVKFEPDYL
DALVMHAANG KLFLDGEFVP G