PTNAB_SHIFL
ID PTNAB_SHIFL Reviewed; 323 AA.
AC P69800; P08186; Q47350;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=PTS system mannose-specific EIIAB component {ECO:0000250|UniProtKB:P69797};
DE EC=2.7.1.191 {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=EIIAB-Man {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=EIII-Man {ECO:0000250|UniProtKB:P69797};
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=PTS system mannose-specific EIIA component {ECO:0000250|UniProtKB:P69797};
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P69797};
DE AltName: Full=PTS system mannose-specific EIIB component {ECO:0000250|UniProtKB:P69797};
GN Name=manX; OrderedLocusNames=SF1411, S1526;
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:P69797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837;
CC EC=2.7.1.191; Evidence={ECO:0000250|UniProtKB:P69797};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P69797}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69797}. Cell
CC inner membrane {ECO:0000250|UniProtKB:P69797}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P69797}.
CC -!- DOMAIN: The PTS EIIA type-4 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-4 domain. {ECO:0000250|UniProtKB:P69797, ECO:0000305}.
CC -!- DOMAIN: The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on
CC a histidyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00424}.
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DR EMBL; AE005674; AAN43012.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16907.1; -; Genomic_DNA.
DR RefSeq; NP_707305.1; NC_004337.2.
DR RefSeq; WP_000150543.1; NZ_UIQL01000067.1.
DR AlphaFoldDB; P69800; -.
DR SMR; P69800; -.
DR STRING; 198214.SF1411; -.
DR PRIDE; P69800; -.
DR EnsemblBacteria; AAN43012; AAN43012; SF1411.
DR EnsemblBacteria; AAP16907; AAP16907; S1526.
DR GeneID; 1024605; -.
DR GeneID; 66674294; -.
DR KEGG; sfl:SF1411; -.
DR KEGG; sfx:S1526; -.
DR PATRIC; fig|198214.7.peg.1663; -.
DR HOGENOM; CLU_074797_0_0_6; -.
DR OMA; EMIFGKQ; -.
DR OrthoDB; 2008912at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00006; PTS_IIA_man; 1.
DR CDD; cd00001; PTS_IIB_man; 1.
DR Gene3D; 3.40.35.10; -; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR013789; PTS_EIIA_man.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR033887; PTS_IIA_man.
DR InterPro; IPR004720; PTS_IIB_sorbose-sp.
DR InterPro; IPR036667; PTS_IIB_sorbose-sp_sf.
DR InterPro; IPR018455; PTS_IIB_sorbose-sp_subgr.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF03830; PTSIIB_sorb; 1.
DR SUPFAM; SSF52728; SSF52728; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR TIGRFAMs; TIGR00824; EIIA-man; 1.
DR TIGRFAMs; TIGR00854; pts-sorbose; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell inner membrane; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..323
FT /note="PTS system mannose-specific EIIAB component"
FT /id="PRO_0000186656"
FT DOMAIN 2..126
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 160..323
FT /note="PTS EIIB type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT REGION 137..155
FT /note="Hinge"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT ACT_SITE 175
FT /note="Pros-phosphohistidine intermediate; for EIIB
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT SITE 89
FT /note="Involved in the phosphoryl transfer between H-10 and
FT H-175"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT MOD_RES 10
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P69797"
FT MOD_RES 175
FT /note="Phosphohistidine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P69797,
FT ECO:0000255|PROSITE-ProRule:PRU00424"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P69797"
SQ SEQUENCE 323 AA; 35048 MW; A446B79421B8C040 CRC64;
MTIAIVIGTH GWAAEQLLKT AEMLLGEQEN VGWIDFVPGE NAETLIEKYN AQLAKLDTTK
GVLFLVDTWG GSPFNAASRI VVDKEHYEVI AGVNIPMLVE TLMARDDDPS FDELVALAVE
TGREGVKALK AKPVEKAAPA PAAAAPKAAP TPAKPMGPND YMVIGLARID DRLIHGQVAT
RWTKETNVSR IIVVSDEVAA DTVRKTLLTQ VAPPGVTAHV VDVAKMIRVY NNPKYAGERV
MLLFTNPTDV ERLVEGGVKI TSVNVGGMAF RQGKTQVNNA VSVDEKDIEA FKKLNARGIE
LEVRKVSTDP KLKMMDLISK IDK
