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PTQA_SHIFL
ID   PTQA_SHIFL              Reviewed;         116 AA.
AC   P69794; P17335; Q47092; Q47093; Q47094; Q57128;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=PTS system N,N'-diacetylchitobiose-specific EIIA component {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=EIIA-Chb {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=EIII-Chb {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=IIIcel {ECO:0000250|UniProtKB:P69791};
DE   AltName: Full=N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69791};
GN   Name=chbA; Synonyms=celC; OrderedLocusNames=SF1490, S1607;
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: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane. The
CC       enzyme II ChbABC PTS system is involved in the transport of the chitin
CC       disaccharide N,N'-diacetylchitobiose (GlcNAc2).
CC       {ECO:0000250|UniProtKB:P69791}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P69791};
CC       Note=Can also use copper and nickel with lower efficiency.
CC       {ECO:0000250|UniProtKB:P69791};
CC   -!- SUBUNIT: Forms a complex with ChbB (EIIB). ChbA is a homotrimer.
CC       {ECO:0000250|UniProtKB:P69791}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By GlcNAc2, GlcNAc3 and beta-N,N'-diacetylchitobiose (Me-
CC       TCB). {ECO:0000250|UniProtKB:P69791}.
CC   -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC       EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR   EMBL; AE005674; AAN43082.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16974.1; -; Genomic_DNA.
DR   RefSeq; NP_707375.2; NC_004337.2.
DR   RefSeq; WP_000968919.1; NZ_WPGW01000081.1.
DR   AlphaFoldDB; P69794; -.
DR   BMRB; P69794; -.
DR   SMR; P69794; -.
DR   STRING; 198214.SF1490; -.
DR   EnsemblBacteria; AAN43082; AAN43082; SF1490.
DR   EnsemblBacteria; AAP16974; AAP16974; S1607.
DR   GeneID; 1026385; -.
DR   GeneID; 67415560; -.
DR   KEGG; sfl:SF1490; -.
DR   KEGG; sfx:S1607; -.
DR   PATRIC; fig|198214.7.peg.1758; -.
DR   HOGENOM; CLU_152490_3_0_6; -.
DR   OrthoDB; 2038379at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd00215; PTS_IIA_lac; 1.
DR   InterPro; IPR003188; PTS_IIA_lac/cel.
DR   InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR   PANTHER; PTHR34382; PTHR34382; 1.
DR   Pfam; PF02255; PTS_IIA; 1.
DR   PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR   SUPFAM; SSF46973; SSF46973; 1.
DR   TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR   PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..116
FT                   /note="PTS system N,N'-diacetylchitobiose-specific EIIA
FT                   component"
FT                   /id="PRO_0000186497"
FT   DOMAIN          15..113
FT                   /note="PTS EIIA type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT   ACT_SITE        89
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P69791"
FT   MOD_RES         89
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
SQ   SEQUENCE   116 AA;  12748 MW;  F2951DC6700FA8A9 CRC64;
     MMDLDNIPDT QTEAEELEEV VMGLIINSGQ ARSLAYAALK QAKQGDFAAA KAMMDQSRMA
     LNEAHLVQTK LIEGDAGEGK MKVSLVLVHA QDHLMTSMLA RELITELIEL HEKLKA
 
 
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