PTNC_SHIFL
ID PTNC_SHIFL Reviewed; 266 AA.
AC P69804; P08187; Q47351;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=PTS system mannose-specific EIIC component {ECO:0000250|UniProtKB:P69801};
DE AltName: Full=EII-P-Man {ECO:0000250|UniProtKB:P69801};
DE AltName: Full=EIIC-Man {ECO:0000250|UniProtKB:P69801};
DE AltName: Full=Mannose permease IIC component {ECO:0000250|UniProtKB:P69801};
GN Name=manY; OrderedLocusNames=SF1410, S1525;
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 ManXYZ PTS system is involved in mannose transport.
CC {ECO:0000250|UniProtKB:P69801}.
CC -!- SUBUNIT: Homotrimer of protomers that are composed of two subunits, IIC
CC and IID. {ECO:0000250|UniProtKB:P69801}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00429}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00429}.
CC -!- DOMAIN: The PTS EIIC type-4 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00429}.
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DR EMBL; AE005674; AAN43011.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16906.1; -; Genomic_DNA.
DR RefSeq; NP_707304.1; NC_004337.2.
DR RefSeq; WP_000406926.1; NZ_WPGW01000062.1.
DR AlphaFoldDB; P69804; -.
DR SMR; P69804; -.
DR STRING; 198214.SF1410; -.
DR EnsemblBacteria; AAN43011; AAN43011; SF1410.
DR EnsemblBacteria; AAP16906; AAP16906; S1525.
DR GeneID; 1024603; -.
DR GeneID; 66674293; -.
DR KEGG; sfl:SF1410; -.
DR KEGG; sfx:S1525; -.
DR PATRIC; fig|198214.7.peg.1662; -.
DR HOGENOM; CLU_069101_0_0_6; -.
DR OMA; LSWIHVS; -.
DR OrthoDB; 1456742at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR InterPro; IPR004700; PTS_IIC_man.
DR Pfam; PF03609; EII-Sor; 1.
DR TIGRFAMs; TIGR00822; EII-Sor; 1.
DR PROSITE; PS51106; PTS_EIIC_TYPE_4; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Formylation; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..266
FT /note="PTS system mannose-specific EIIC component"
FT /id="PRO_0000186649"
FT TOPO_DOM 1..4
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT INTRAMEM 5..43
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 44..46
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT INTRAMEM 47..86
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 87..90
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TRANSMEM 91..124
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 125..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TRANSMEM 133..160
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 161..176
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TRANSMEM 177..200
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 201..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TRANSMEM 208..218
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 219..224
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TRANSMEM 225..242
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT TOPO_DOM 243..266
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P69801"
FT DOMAIN 1..237
FT /note="PTS EIIC type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P69801"
SQ SEQUENCE 266 AA; 27636 MW; EAFDD9E4B809AF23 CRC64;
MEITTLQIVL VFIVACIAGM GSILDEFQFH RPLIACTLVG IVLGDMKTGI IIGGTLEMIA
LGWMNIGAAV APDAALASII STILVIAGHQ SIGAGIALAI PLAAAGQVLT IIVRTITVAF
QHAADKAADN GNLTAISWIH VSSLFLQAMR VAIPAVIVAL SVGTSEVQNM LNAIPEVVTN
GLNIAGGMIV VVGYAMVINM MRAGYLMPFF YLGFVTAAFT NFNLVALGVI GTVMAVLYIQ
LSPKYNRVAG APAQAAGNND LDNELD
