ID   AIS_SHIF8               Reviewed;         200 AA.
AC   Q0T2N1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 74.
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=SFV_2322;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(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=ABF04434.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000266; ABF04434.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_024260288.1; NC_008258.1.
DR   AlphaFoldDB; Q0T2N1; -.
DR   SMR; Q0T2N1; -.
DR   EnsemblBacteria; ABF04434; ABF04434; SFV_2322.
DR   KEGG; sfv:SFV_2322; -.
DR   HOGENOM; CLU_106705_1_0_6; -.
DR   BioCyc; SFLE373384:SFV_RS12980-MON; -.
DR   UniPathway; UPA00451; -.
DR   Proteomes; UP000000659; 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_0000380589"
SQ   SEQUENCE   200 AA;  22320 MW;  B09D47DC1CF7F59E CRC64;
     MLAFCRSSLK SKKYFIILLA LAAIAGLGTH AAWSSNGLPR IDNKTLARLA QQHPVVVLFR
     HAERCDRSTN QCLSDKTGIT VKGTQDAREL GNAFSADIPD FDLYSSNTVR TIQSATWFSA
     GKKLTVDKRL LQCGNEIYSA IKDLQSKAPD KNIVIFTHNH CMTYIAKNKR DAIFKPDYLD
     GLVMHVEKGK VYLDGEFVNH