ID PTNAB_ECOLI Reviewed; 323 AA.
AC P69797; P08186; Q47350;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 24-JAN-2024, entry version 158.
DE RecName: Full=PTS system mannose-specific EIIAB component {ECO:0000303|PubMed:8262947};
DE EC=2.7.1.191 {ECO:0000269|PubMed:2681202, ECO:0000269|PubMed:8262947};
DE AltName: Full=EIIAB-Man {ECO:0000303|PubMed:8262947};
DE AltName: Full=EIII-Man {ECO:0000303|PubMed:2951378};
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:8262947};
DE AltName: Full=PTS system mannose-specific EIIA component {ECO:0000303|PubMed:8262947};
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:8262947};
DE AltName: Full=PTS system mannose-specific EIIB component {ECO:0000303|PubMed:8262947};
GN Name=manX {ECO:0000303|Ref.1};
GN Synonyms=gptB, ptsL {ECO:0000303|PubMed:2951378};
GN OrderedLocusNames=b1817, JW1806;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Saris P.E.J., Liljestroem P., Palva E.T.;
RT "Nucleotide sequence of manX(ptsL) encoding the enzyme III(Man) (II-A(Man))
RT function in the phosphotransferase system of Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 49:69-73(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP SUBUNIT.
RX PubMed=2951378; DOI=10.1016/s0021-9258(18)61180-9;
RA Erni B., Zanolari B., Kocher H.P.;
RT "The mannose permease of Escherichia coli consists of three different
RT proteins. Amino acid sequence and function in sugar transport, sugar
RT phosphorylation, and penetration of phage lambda DNA.";
RL J. Biol. Chem. 262:5238-5247(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [4]
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 [5]
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 [6]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP FUNCTION.
RX PubMed=4604906; DOI=10.1073/pnas.71.7.2895;
RA Adler J., Epstein W.;
RT "Phosphotransferase-system enzymes as chemoreceptors for certain sugars in
RT Escherichia coli chemotaxis.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:2895-2899(1974).
RN [8]
RP FUNCTION.
RX PubMed=353494; DOI=10.1007/bf00266608;
RA Elliott J., Arber W.;
RT "E. coli K-12 pel mutants, which block phage lambda DNA injection, coincide
RT with ptsM, which determines a component of a sugar transport system.";
RL Mol. Gen. Genet. 161:1-8(1978).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=2999119; DOI=10.1016/s0021-9258(17)36282-8;
RA Erni B., Zanolari B.;
RT "The mannose-permease of the bacterial phosphotransferase system. Gene
RT cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia
RT coli.";
RL J. Biol. Chem. 260:15495-15503(1985).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PHOSPHORYLATION AT HIS-10 AND
RP HIS-175.
RX PubMed=2681202; DOI=10.1016/s0021-9258(18)51529-5;
RA Erni B., Zanolari B., Graff P., Kocher H.P.;
RT "Mannose permease of Escherichia coli. Domain structure and function of the
RT phosphorylating subunit.";
RL J. Biol. Chem. 264:18733-18741(1989).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-10; TRP-12; LYS-48;
RP SER-72; HIS-86; SER-110; HIS-175 AND HIS-219, ACTIVE SITE, PHOSPHORYLATION
RP AT HIS-10 AND HIS-175, AND SUBUNIT.
RX PubMed=8262947; DOI=10.1016/s0021-9258(19)74222-7;
RA Stolz B., Huber M., Markovic-Housley Z., Erni B.;
RT "The mannose transporter of Escherichia coli. Structure and function of the
RT IIABMan subunit.";
RL J. Biol. Chem. 268:27094-27099(1993).
RN [12]
RP INDUCTION.
RX PubMed=9484892; DOI=10.1046/j.1365-2958.1998.00685.x;
RA Plumbridge J.;
RT "Control of the expression of the manXYZ operon in Escherichia coli: Mlc is
RT a negative regulator of the mannose PTS.";
RL Mol. Microbiol. 27:369-380(1998).
RN [13]
RP INDUCTION.
RX PubMed=11361067;
RA Plumbridge J.;
RT "Regulation of PTS gene expression by the homologous transcriptional
RT regulators, Mlc and NagC, in Escherichia coli (or how two similar
RT repressors can behave differently).";
RL J. Mol. Microbiol. Biotechnol. 3:371-380(2001).
RN [14]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-234, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [16]
RP REVIEW.
RX PubMed=32710850; DOI=10.1016/j.bbamem.2020.183412;
RA Jeckelmann J.M., Erni B.;
RT "The mannose phosphotransferase system (Man-PTS) - Mannose transporter and
RT receptor for bacteriocins and bacteriophages.";
RL Biochim. Biophys. Acta 1862:183412-183412(2020).
RN [17] {ECO:0007744|PDB:1PDO}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-134, DOMAIN, AND ACTIVE SITE.
RX PubMed=8676384; DOI=10.1006/jmbi.1996.0335;
RA Nunn R.S., Markovic-Housley Z., Genovesio-Taverne J.-C., Fluekiger K.,
RA Rizkallah P.J., Jansonius J.N., Schirmer T., Erni B.;
RT "Structure of the IIA domain of the mannose transporter from Escherichia
RT coli at 1.7-A resolution.";
RL J. Mol. Biol. 259:502-511(1996).
RN [18]
RP STRUCTURE BY NMR OF 1-121.
RX PubMed=8131846; DOI=10.1016/0014-5793(94)80138-x;
RA Markovic-Housley Z., Balbach J., Stolz B., Genovesio-Taverne J.-C.;
RT "Predicted topology of the N-terminal domain of the hydrophilic subunit of
RT the mannose transporter of Escherichia coli.";
RL FEBS Lett. 340:202-206(1994).
RN [19]
RP STRUCTURE BY NMR OF 156-323.
RX PubMed=9074635; DOI=10.1016/s0014-5793(97)00084-7;
RA Gschwind R.M., Gemmecker G., Leutner M., Kessler H., Gutknecht R., Lanz R.,
RA Fluekiger K., Erni B.;
RT "Secondary structure of the IIB domain of the Escherichia coli mannose
RT transporter, a new fold in the class of alpha/beta twisted open-sheet
RT structures.";
RL FEBS Lett. 404:45-50(1997).
RN [20] {ECO:0007744|PDB:1VRC}
RP STRUCTURE BY NMR OF 1-133, SUBUNIT, AND ACTIVE SITE.
RX PubMed=15788390; DOI=10.1074/jbc.m501986200;
RA Williams D.C. Jr., Cai M., Suh J.Y., Peterkofsky A., Clore G.M.;
RT "Solution NMR structure of the 48-kDa IIAMannose-HPr complex of the
RT Escherichia coli mannose phosphotransferase system.";
RL J. Biol. Chem. 280:20775-20784(2005).
RN [21] {ECO:0007744|PDB:1VSQ, ECO:0007744|PDB:2JZH, ECO:0007744|PDB:2JZN, ECO:0007744|PDB:2JZO}
RP STRUCTURE BY NMR OF 2-134 AND 159-323, MUTAGENESIS OF HIS-10, DOMAIN, AND
RP ACTIVE SITE.
RX PubMed=18270202; DOI=10.1074/jbc.m800312200;
RA Hu J., Hu K., Williams D.C. Jr., Komlosh M.E., Cai M., Clore G.M.;
RT "Solution NMR structures of productive and non-productive complexes between
RT the A and B domains of the cytoplasmic subunit of the mannose transporter
RT of the Escherichia coli phosphotransferase system.";
RL J. Biol. Chem. 283:11024-11037(2008).
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:0000269|PubMed:2681202, ECO:0000269|PubMed:2951378,
CC ECO:0000269|PubMed:2999119, ECO:0000269|PubMed:8262947}.
CC -!- FUNCTION: Also functions as a receptor for bacterial chemotaxis and is
CC required for infection of the cell by bacteriophage lambda where it
CC most likely functions as a pore for penetration of lambda DNA.
CC {ECO:0000269|PubMed:353494, ECO:0000269|PubMed:4604906}.
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:0000269|PubMed:2681202,
CC ECO:0000269|PubMed:8262947};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15788390,
CC ECO:0000269|PubMed:2681202, ECO:0000269|PubMed:2951378,
CC ECO:0000269|PubMed:2999119, ECO:0000305|PubMed:8262947}.
CC -!- INTERACTION:
CC P69797; P0ACN7: cytR; NbExp=2; IntAct=EBI-554089, EBI-1125696;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119}. Cell inner
CC membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:2999119};
CC Peripheral membrane protein {ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:2999119}.
CC -!- INDUCTION: Expression of the manXYZ operon is positively regulated by
CC the cAMP-CRP complex and negatively regulated by the Mlc
CC transcriptional repressor (PubMed:9484892, PubMed:11361067). Expression
CC is also weakly repressed by NagC (PubMed:9484892, PubMed:11361067).
CC {ECO:0000269|PubMed:11361067, ECO:0000269|PubMed:9484892}.
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:0000255|PROSITE-ProRule:PRU00419,
CC ECO:0000305|PubMed:18270202, ECO:0000305|PubMed:8676384}.
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,
CC ECO:0000305|PubMed:18270202}.
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DR EMBL; M36404; AAA24110.1; -; Genomic_DNA.
DR EMBL; J02699; AAA24443.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74887.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15624.1; -; Genomic_DNA.
DR PIR; A30286; WQECM3.
DR RefSeq; NP_416331.1; NC_000913.3.
DR RefSeq; WP_000150543.1; NZ_STEB01000009.1.
DR PDB; 1PDO; X-ray; 1.70 A; A=2-133.
DR PDB; 1VRC; NMR; -; A/B=1-133.
DR PDB; 1VSQ; NMR; -; A/B=2-134, C=159-323.
DR PDB; 2JZH; NMR; -; A=154-323.
DR PDB; 2JZN; NMR; -; A/B=2-134, C=159-323.
DR PDB; 2JZO; NMR; -; A/B=2-134, D=159-323.
DR PDBsum; 1PDO; -.
DR PDBsum; 1VRC; -.
DR PDBsum; 1VSQ; -.
DR PDBsum; 2JZH; -.
DR PDBsum; 2JZN; -.
DR PDBsum; 2JZO; -.
DR AlphaFoldDB; P69797; -.
DR SMR; P69797; -.
DR BioGRID; 4259144; 308.
DR BioGRID; 850691; 2.
DR ComplexPortal; CPX-5968; D-mannose-specific enzyme II complex.
DR DIP; DIP-35846N; -.
DR IntAct; P69797; 15.
DR MINT; P69797; -.
DR STRING; 511145.b1817; -.
DR TCDB; 4.A.6.1.1; the pts mannose-fructose-sorbose (man) family.
DR iPTMnet; P69797; -.
DR SWISS-2DPAGE; P69797; -.
DR jPOST; P69797; -.
DR PaxDb; 511145-b1817; -.
DR EnsemblBacteria; AAC74887; AAC74887; b1817.
DR GeneID; 75202643; -.
DR GeneID; 946334; -.
DR KEGG; ecj:JW1806; -.
DR KEGG; eco:b1817; -.
DR PATRIC; fig|1411691.4.peg.434; -.
DR EchoBASE; EB0562; -.
DR eggNOG; COG2893; Bacteria.
DR eggNOG; COG3444; Bacteria.
DR HOGENOM; CLU_074797_0_0_6; -.
DR InParanoid; P69797; -.
DR OMA; EMIFGKQ; -.
DR OrthoDB; 7065728at2; -.
DR PhylomeDB; P69797; -.
DR BioCyc; EcoCyc:MANX-MONOMER; -.
DR BioCyc; MetaCyc:MANX-MONOMER; -.
DR EvolutionaryTrace; P69797; -.
DR PRO; PR:P69797; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IPI:ComplexPortal.
DR GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR GO; GO:0022870; F:protein-N(PI)-phosphohistidine-mannose phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0098708; P:glucose import across plasma membrane; IDA:EcoCyc.
DR GO; GO:0015761; P:mannose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:ComplexPortal.
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; 3.40.50.510; Phosphotransferase system, mannose-type IIA component; 1.
DR Gene3D; 3.40.35.10; Phosphotransferase system, sorbose subfamily IIB component; 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 NCBIfam; TIGR00824; EIIA-man; 1.
DR NCBIfam; TIGR00854; pts-sorbose; 1.
DR PANTHER; PTHR33799:SF1; PHOSPHOTRANSFERASE ENZYME IIA COMPONENT YADI-RELATED; 1.
DR PANTHER; PTHR33799; PTS PERMEASE-RELATED-RELATED; 1.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF03830; PTSIIB_sorb; 1.
DR SUPFAM; SSF52728; PTS IIb component; 1.
DR SUPFAM; SSF53062; PTS system fructose IIA component-like; 1.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell inner membrane; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646,
FT ECO:0000305|PubMed:2951378"
FT CHAIN 2..323
FT /note="PTS system mannose-specific EIIAB component"
FT /id="PRO_0000186653"
FT DOMAIN 2..124
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000305|PubMed:18270202, ECO:0000305|PubMed:8676384"
FT DOMAIN 157..320
FT /note="PTS EIIB type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424,
FT ECO:0000305|PubMed:18270202"
FT REGION 137..155
FT /note="Hinge"
FT /evidence="ECO:0000305|PubMed:2681202"
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT ECO:0000305|PubMed:15788390, ECO:0000305|PubMed:18270202,
FT ECO:0000305|PubMed:8262947, ECO:0000305|PubMed:8676384"
FT ACT_SITE 175
FT /note="Pros-phosphohistidine intermediate; for EIIB
FT activity"
FT /evidence="ECO:0000305|PubMed:18270202,
FT ECO:0000305|PubMed:8262947"
FT SITE 89
FT /note="Involved in the phosphoryl transfer between H-10 and
FT H-175"
FT /evidence="ECO:0000305|PubMed:8262947"
FT MOD_RES 10
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305|PubMed:2681202,
FT ECO:0000305|PubMed:8262947"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 175
FT /note="Phosphohistidine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424,
FT ECO:0000305|PubMed:2681202, ECO:0000305|PubMed:8262947"
FT MOD_RES 234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 10
FT /note="H->C: Loss of phosphotransferase activity. Unable to
FT dimerize."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 10
FT /note="H->E: Results in the formation of a single complex
FT corresponding to the productive phosphoryl transfer
FT complex."
FT /evidence="ECO:0000269|PubMed:18270202"
FT MUTAGEN 12
FT /note="W->F: Slight phosphotransferase activity. Unable to
FT dimerize."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 48
FT /note="K->C: Retains more than 50% of phosphotransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 72
FT /note="S->C: Slight phosphotransferase activity. Unable to
FT dimerize."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 86
FT /note="H->N: Loss of phosphotransferase activity."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 110
FT /note="S->C: Retains more than 50% of phosphotransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 175
FT /note="H->C: Loss of phosphotransferase activity."
FT /evidence="ECO:0000269|PubMed:8262947"
FT MUTAGEN 219
FT /note="H->Q: Slight phosphotransferase activity."
FT /evidence="ECO:0000269|PubMed:8262947"
FT CONFLICT 2..23
FT /note="TIAIVIGTHGWAAEQLLKTAEM -> GWGCRAGCLKRQKW (in Ref. 1;
FT AAA24110)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="D -> N (in Ref. 1; AAA24110)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="T -> R (in Ref. 1; AAA24110)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="A -> G (in Ref. 1; AAA24110)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:1PDO"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:1VRC"
FT HELIX 13..25
FT /evidence="ECO:0007829|PDB:1PDO"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1PDO"
FT HELIX 42..53
FT /evidence="ECO:0007829|PDB:1PDO"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:1PDO"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:1PDO"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:1PDO"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1PDO"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:1PDO"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 202..210
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 239..246
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 247..255
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 285..296
FT /evidence="ECO:0007829|PDB:1VSQ"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1VSQ"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1VSQ"
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
//
