NANS_ECOLI
ID NANS_ECOLI Reviewed; 326 AA.
AC P39370; Q2M604;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable 9-O-acetyl-N-acetylneuraminic acid deacetylase;
DE Short=Neu5,9Ac2 deacetylase;
DE EC=3.1.1.-;
DE AltName: Full=Probable 9-O-acetyl-N-acetylneuraminate esterase;
DE AltName: Full=Probable sialyl esterase NanS;
DE Flags: Precursor;
GN Name=nanS; Synonyms=yjhS; OrderedLocusNames=b4309, JW4272;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP INDUCTION BY N-ACETYLNEURAMINATE.
RX PubMed=15743943; DOI=10.1128/jb.187.6.1959-1965.2005;
RA Condemine G., Berrier C., Plumbridge J., Ghazi A.;
RT "Function and expression of an N-acetylneuraminic acid-inducible outer
RT membrane channel in Escherichia coli.";
RL J. Bacteriol. 187:1959-1965(2005).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / BW30270;
RX PubMed=19749043; DOI=10.1128/jb.01000-09;
RA Steenbergen S.M., Jirik J.L., Vimr E.R.;
RT "YjhS (NanS) is required for Escherichia coli to grow on 9-O-acetylated N-
RT acetylneuraminic acid.";
RL J. Bacteriol. 191:7134-7139(2009).
RN [6]
RP INDUCTION.
RX PubMed=23935044; DOI=10.1128/jb.00692-13;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT NanR.";
RL J. Bacteriol. 195:4689-4701(2013).
CC -!- FUNCTION: Probably catalyzes the hydrolysis of the 9-O-acetyl group of
CC 9-O-acetyl-N-acetylneuraminate (Neu5,9Ac2). Is required for growth of
CC E.coli on Neu5,9Ac2, an alternative sialic acid commonly found in
CC mammalian host mucosal sites, in particular in the human intestine.
CC {ECO:0000269|PubMed:19749043}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:19749043}.
CC -!- INDUCTION: Induced by N-acetylneuraminate and modulated by N-
CC acetylglucosamine, via the NanR and NagC regulators.
CC {ECO:0000269|PubMed:23935044, ECO:0000305|PubMed:15743943}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene cannot grow on Neu5,9Ac2
CC as the sole carbon source, in contrast to wild-type, but grow as well
CC as wild-type on glycerol or on N-acetylneuraminate (Neu5Ac).
CC {ECO:0000269|PubMed:19749043}.
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DR EMBL; U14003; AAA97205.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77265.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78302.1; -; Genomic_DNA.
DR PIR; S56534; S56534.
DR RefSeq; NP_418729.1; NC_000913.3.
DR RefSeq; WP_000991438.1; NZ_SSUV01000012.1.
DR AlphaFoldDB; P39370; -.
DR SMR; P39370; -.
DR BioGRID; 4259373; 13.
DR DIP; DIP-12627N; -.
DR STRING; 511145.b4309; -.
DR PaxDb; P39370; -.
DR PRIDE; P39370; -.
DR EnsemblBacteria; AAC77265; AAC77265; b4309.
DR EnsemblBacteria; BAE78302; BAE78302; BAE78302.
DR GeneID; 948835; -.
DR KEGG; ecj:JW4272; -.
DR KEGG; eco:b4309; -.
DR PATRIC; fig|1411691.4.peg.2384; -.
DR EchoBASE; EB2449; -.
DR eggNOG; ENOG502ZIWU; Bacteria.
DR HOGENOM; CLU_014323_0_1_6; -.
DR InParanoid; P39370; -.
DR OMA; ARFTHTH; -.
DR BioCyc; EcoCyc:G7919-MON; -.
DR BioCyc; MetaCyc:G7919-MON; -.
DR BRENDA; 3.1.1.53; 2026.
DR PRO; PR:P39370; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0001681; F:sialate O-acetylesterase activity; IDA:EcoCyc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IMP:EcoCyc.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; IMP:EcoCyc.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR005181; SASA.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF03629; SASA; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Hydrolase; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..326
FT /note="Probable 9-O-acetyl-N-acetylneuraminic acid
FT deacetylase"
FT /id="PRO_0000013942"
SQ SEQUENCE 326 AA; 36878 MW; 6E48217701678DAD CRC64;
MNAIISPDYY YVLTVAGQSN AMAYGEGLPL PDREDAPHPR IKQLARFAHT HPGGPPCHFN
DIIPLTHCPH DVQDMQGYHH PLATNHQTQY GTVGQALHIA RKLLPFIPDN AGILIVPCCR
GGSAFTAGSE GTYSERHGAS HDACRWGTDT PLYQDLVSRT RAALAKNPQN KFLGACWMQG
EFDLMTSDYA SHPQHFNHMV EAFRRDLKQY HSQLNNITDA PWFCGDTTWY WKENFPHSYE
AIYGNYQNNV LANIIFVDFQ QQGERGLTNA PDEDPDDLST GYYGSAYRSP ENWTTALRSS
HFSTAARRGI ISDRFVEAIL QFWRER
