AIS_SHIFL
ID AIS_SHIFL Reviewed; 200 AA.
AC Q83QU0; Q7UC65;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 5.
DT 25-MAY-2022, entry version 106.
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};
GN OrderedLocusNames=SF2331, S2464;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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=AAN43845.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP17664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43845.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17664.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_708138.2; NC_004337.2.
DR RefSeq; WP_005098986.1; NZ_UIQL01000041.1.
DR AlphaFoldDB; Q83QU0; -.
DR SMR; Q83QU0; -.
DR STRING; 198214.SF2331; -.
DR EnsemblBacteria; AAN43845; AAN43845; SF2331.
DR EnsemblBacteria; AAP17664; AAP17664; S2464.
DR GeneID; 1027258; -.
DR KEGG; sfl:SF2331; -.
DR KEGG; sft:NCTC1_02564; -.
DR KEGG; sfx:S2464; -.
DR PATRIC; fig|198214.7.peg.2793; -.
DR HOGENOM; CLU_106705_1_0_6; -.
DR OrthoDB; 1642854at2; -.
DR UniPathway; UPA00451; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; 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_0000380588"
SQ SEQUENCE 200 AA; 22292 MW; 36477B2C23F50BE7 CRC64;
MLAFCRSSLK SKKYFIILLA LAAIAGLGTH AAWSSNGLPR IDNKTLARLA QQHPVVVLFR
HAERCDRSTN QCLSDKTGIT VKGTQDAREL GNAFSADISD FDLYSSNTVR TIQSATWFSA
GKKLTVDKRL LQCGNEIYSA IKDLQSKAPD KNIVIFTHNH CLTYIAKNKR DAIFKPDYLD
GLVMHVEKGK VYLDGEFVNH