ID AIS_SALPB Reviewed; 201 AA.
AC A9N5B6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=SPAB_00686;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., 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; CP000886; ABX66112.1; -; Genomic_DNA.
DR RefSeq; WP_000879248.1; NC_010102.1.
DR AlphaFoldDB; A9N5B6; -.
DR SMR; A9N5B6; -.
DR KEGG; spq:SPAB_00686; -.
DR PATRIC; fig|1016998.12.peg.646; -.
DR HOGENOM; CLU_106705_1_0_6; -.
DR BioCyc; SENT1016998:SPAB_RS02855-MONOMER; -.
DR UniPathway; UPA00451; -.
DR Proteomes; UP000008556; 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..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_0000380582"
SQ SEQUENCE 201 AA; 22027 MW; A34132FD78210504 CRC64;
MLAFTLRFIK NKRYFAILAG ALVIIAGLTS QHAWSGNGLP QINGKALAAL AKQHPVVVLF
RHAERCDRSD NTCLSDSTGI TVKGAQDARA LGKAFSADIQ NYNLYSSNTV RTIQSATWFS
AGRSLTVDKK MMDCGSGIYA SINTLLKKSQ NKNIVIFTHN HCLTYIAKNK RGVKFDPDYL
NALVMHAENG KLFLDGEFVP G
//
