MNGA_ECOLI
ID MNGA_ECOLI Reviewed; 658 AA.
AC P54745;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component {ECO:0000303|PubMed:14645248};
DE AltName: Full=2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme MngA {ECO:0000303|PubMed:14645248};
DE AltName: Full=Protein-Npi-phosphohistidine--2-O-alpha-mannosyl-D-glycerate phosphotransferase {ECO:0000303|PubMed:14645248};
DE Includes:
DE RecName: Full=2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:14645248};
DE AltName: Full=PTS system EIIA component {ECO:0000303|PubMed:14645248};
DE Includes:
DE RecName: Full=2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:14645248};
DE EC=2.7.1.195 {ECO:0000269|PubMed:14645248};
DE AltName: Full=PTS system EIIB component {ECO:0000303|PubMed:14645248};
DE Includes:
DE RecName: Full=2-O-alpha-mannosyl-D-glycerate-specific permease IIC component {ECO:0000303|PubMed:14645248};
DE AltName: Full=PTS system EIIC component {ECO:0000303|PubMed:14645248};
GN Name=mngA {ECO:0000303|PubMed:14645248};
GN Synonyms=hrsA {ECO:0000303|PubMed:9063979};
GN OrderedLocusNames=b0731, JW0720;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND ACTIVE SITE.
RX PubMed=9063979; DOI=10.1271/bbb.60.309;
RA Utsumi R., Horie T., Katoh A., Kaino Y., Tanabe H., Noda M.;
RT "Isolation and characterization of the heat-responsive genes in Escherichia
RT coli.";
RL Biosci. Biotechnol. Biochem. 60:309-315(1996).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 277-658.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14645248; DOI=10.1074/jbc.m310980200;
RA Sampaio M.-M., Chevance F., Dippel R., Eppler T., Schlegel A., Boos W.,
RA Lu Y.-J., Rock C.O.;
RT "Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-
RT D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA)
RT gene and is regulated by the mngR (farR) gene product acting as
RT repressor.";
RL J. Biol. Chem. 279:5537-5548(2004).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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
CC (PubMed:14645248, PubMed:9063979). This system is involved in mannosyl-
CC D-glycerate transport (PubMed:14645248). Also involved in
CC thermoinduction of ompC (PubMed:9063979). {ECO:0000269|PubMed:14645248,
CC ECO:0000269|PubMed:9063979}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-
CC L-histidyl-[protein] = (2R)-2-O-(6-phospho-alpha-D-mannosyl)-
CC glycerate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33307,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:29979,
CC ChEBI:CHEBI:57541, ChEBI:CHEBI:60331, ChEBI:CHEBI:64837;
CC EC=2.7.1.195; Evidence={ECO:0000269|PubMed:14645248};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for mannosyl-D-glycerate {ECO:0000269|PubMed:14645248};
CC Vmax=0.65 nmol/min/mg enzyme for mannosyl-D-glycerate
CC {ECO:0000269|PubMed:14645248};
CC -!- INTERACTION:
CC P54745; P0ACA3: sspA; NbExp=5; IntAct=EBI-558542, EBI-558482;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427, ECO:0000305|PubMed:14645248}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00427,
CC ECO:0000305|PubMed:14645248}.
CC -!- INDUCTION: Induced by mannosyl-D-glycerate. Repressed by MngR.
CC {ECO:0000269|PubMed:14645248}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to transport
CC mannosyl-D-glycerate. {ECO:0000269|PubMed:14645248}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D64014; BAA10893.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73825.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35397.2; -; Genomic_DNA.
DR PIR; JC4598; JC4598.
DR RefSeq; NP_415259.1; NC_000913.3.
DR RefSeq; WP_000242633.1; NZ_CP011343.2.
DR AlphaFoldDB; P54745; -.
DR SMR; P54745; -.
DR BioGRID; 4263541; 15.
DR BioGRID; 849731; 1.
DR DIP; DIP-9939N; -.
DR IntAct; P54745; 1.
DR STRING; 511145.b0731; -.
DR TCDB; 4.A.2.1.3; the pts fructose-mannitol (fru) family.
DR PaxDb; P54745; -.
DR PRIDE; P54745; -.
DR EnsemblBacteria; AAC73825; AAC73825; b0731.
DR EnsemblBacteria; BAA35397; BAA35397; BAA35397.
DR GeneID; 945355; -.
DR KEGG; ecj:JW0720; -.
DR KEGG; eco:b0731; -.
DR PATRIC; fig|511145.12.peg.761; -.
DR EchoBASE; EB3024; -.
DR eggNOG; COG1299; Bacteria.
DR eggNOG; COG1445; Bacteria.
DR eggNOG; COG1762; Bacteria.
DR HOGENOM; CLU_013155_1_2_6; -.
DR OMA; QENSWLW; -.
DR PhylomeDB; P54745; -.
DR BioCyc; EcoCyc:HRSA-MON; -.
DR BioCyc; MetaCyc:HRSA-MON; -.
DR BRENDA; 2.7.1.195; 2026.
DR PRO; PR:P54745; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
DR GO; GO:0090581; F:protein-phosphocysteine-mannosylglycerate-phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; ISM:EcoCyc.
DR GO; GO:0051476; P:phosphoenolpyruvate-dependent mannosylglycerate phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05569; PTS_IIB_fructose; 1.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013014; PTS_EIIC_2.
DR InterPro; IPR004715; PTS_IIA_fruc.
DR InterPro; IPR003353; PTS_IIB_fruc.
DR InterPro; IPR006327; PTS_IIC_fruc.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00829; FRU; 1.
DR TIGRFAMs; TIGR00848; fruA; 1.
DR TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..658
FT /note="PTS system 2-O-alpha-mannosyl-D-glycerate-specific
FT EIIABC component"
FT /id="PRO_0000186699"
FT TOPO_DOM 1..313
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 335..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 380..389
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 411..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 455..474
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 475..495
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 496..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 522..551
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 595..620
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT TOPO_DOM 642..658
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..171
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT DOMAIN 186..282
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 306..641
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT ACT_SITE 87
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:9063979"
FT ACT_SITE 192
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305|PubMed:9063979"
FT MOD_RES 87
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305"
FT MOD_RES 192
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422,
FT ECO:0000305"
SQ SEQUENCE 658 AA; 69668 MW; C1F0999A1C48C5C2 CRC64;
MVLFYRAHWR DYKNDQVRIM MNLTTLTHRD ALCLNARFTS REEAIHALTQ RLAALGKISS
TEQFLEEVYR RESLGPTALG EGLAVPHGKT AAVKEAAFAV ATLSEPLQWE GVDGPEAVDL
VVLLAIPPNE AGTTHMQLLT ALTTRLADDE IRARIQSATT PDELLSALDD KGGTQPSASF
SNAPTIVCVT ACPAGIAHTY MAAEYLEKAG RKLGVNVYVE KQGANGIEGR LTADQLNSAT
ACIFAAEVAI KESERFNGIP ALSVPVAEPI RHAEALIQQA LTLKRSDETR TVQQDTQPVK
SVKTELKQAL LSGISFAVPL IVAGGTVLAV AVLLSQIFGL QDLFNEENSW LWMYRKLGGG
LLGILMVPVL AAYTAYSLAD KPALAPGFAA GLAANMIGSG FLGAVVGGLI AGYLMRWVKN
HLRLSSKFNG FLTFYLYPVL GTLGAGSLML FVVGEPVAWI NNSLTAWLNG LSGSNALLLG
AILGFMCSFD LGGPVNKAAY AFCLGAMANG VYGPYAIFAS VKMVSAFTVT ASTMLAPRLF
KEFEIETGKS TWLLGLAGIT EGAIPMAIED PLRVIGSFVL GSMVTGAIVG AMNIGLSTPG
AGIFSLFLLH DNGAGGVMAA IGWFGAALVG AAISTAILLM WRRHAVKHGN YLTDGVMP
