UHPB_ECOLI
ID UHPB_ECOLI Reviewed; 500 AA.
AC P09835; P76729; Q2M7Y1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase UhpB {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:11053370, ECO:0000269|PubMed:11739766};
DE EC=3.1.3.- {ECO:0000269|PubMed:11739766};
GN Name=uhpB {ECO:0000303|PubMed:3038843}; OrderedLocusNames=b3668, JW3643;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3301805; DOI=10.1128/jb.169.8.3556-3563.1987;
RA Friedrich M.J., Kadner R.J.;
RT "Nucleotide sequence of the uhp region of Escherichia coli.";
RL J. Bacteriol. 169:3556-3563(1987).
RN [2]
RP SEQUENCE REVISION.
RA Kadner R.J.;
RL Submitted (AUG-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1569007; DOI=10.1128/jb.174.9.2754-2762.1992;
RA Island M.D., Wei B.-Y., Kadner R.J.;
RT "Structure and function of the uhp genes for the sugar phosphate transport
RT system in Escherichia coli and Salmonella typhimurium.";
RL J. Bacteriol. 174:2754-2762(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [5]
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 [6]
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 [7]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=3038843; DOI=10.1128/jb.169.8.3546-3555.1987;
RA Weston L.A., Kadner R.J.;
RT "Identification of uhp polypeptides and evidence for their role in
RT exogenous induction of the sugar phosphate transport system of Escherichia
RT coli K-12.";
RL J. Bacteriol. 169:3546-3555(1987).
RN [8]
RP FUNCTION.
RX PubMed=8349544; DOI=10.1128/jb.175.16.5028-5034.1993;
RA Island M.D., Kadner R.J.;
RT "Interplay between the membrane-associated UhpB and UhpC regulatory
RT proteins.";
RL J. Bacteriol. 175:5028-5034(1993).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PHOSPHORYLATION AT
RP HIS-313, AND MUTAGENESIS OF HIS-313.
RX PubMed=11053370; DOI=10.1128/jb.182.22.6279-6286.2000;
RA Wright J.S., Olekhnovich I.N., Touchie G., Kadner R.J.;
RT "The histidine kinase domain of UhpB inhibits UhpA action at the
RT Escherichia coli uhpT promoter.";
RL J. Bacteriol. 182:6279-6286(2000).
RN [10]
RP FUNCTION AS A KINASE AND A PHOSPHATASE, CATALYTIC ACTIVITY, AND
RP AUTOPHOSPHORYLATION.
RX PubMed=11739766; DOI=10.1099/00221287-147-12-3345;
RA Verhamme D.T., Arents J.C., Postma P.W., Crielaard W., Hellingwerf K.J.;
RT "Glucose-6-phosphate-dependent phosphoryl flow through the Uhp two-
RT component regulatory system.";
RL Microbiology 147:3345-3352(2001).
RN [11]
RP SUBCELLULAR LOCATION.
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: Part of the UhpABC signaling cascade that controls the
CC expression of the hexose phosphate transporter UhpT. UhpB functions as
CC a membrane-associated protein kinase that autophosphorylates in
CC response to interaction with UhpC, and subsequently transfers its
CC phosphate group to the response regulator UhpA (PubMed:3038843,
CC PubMed:8349544, PubMed:11053370, PubMed:11739766). Can also
CC dephosphorylate UhpA (PubMed:11053370, PubMed:11739766).
CC {ECO:0000269|PubMed:11053370, ECO:0000269|PubMed:11739766,
CC ECO:0000269|PubMed:3038843, ECO:0000269|PubMed:8349544}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:11053370,
CC ECO:0000269|PubMed:11739766};
CC -!- ACTIVITY REGULATION: Kinase activity is stimulated by UhpC.
CC {ECO:0000269|PubMed:11053370}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:11053370,
CC ECO:0000269|PubMed:11739766}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA62020.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M17102; AAA24721.1; -; Genomic_DNA.
DR EMBL; M89479; AAA24725.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62020.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76691.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77625.1; -; Genomic_DNA.
DR PIR; E65168; RGECUB.
DR RefSeq; NP_418124.4; NC_000913.3.
DR RefSeq; WP_001295243.1; NZ_STEB01000015.1.
DR AlphaFoldDB; P09835; -.
DR SMR; P09835; -.
DR BioGRID; 4262583; 21.
DR DIP; DIP-11083N; -.
DR STRING; 511145.b3668; -.
DR iPTMnet; P09835; -.
DR PaxDb; P09835; -.
DR PRIDE; P09835; -.
DR EnsemblBacteria; AAC76691; AAC76691; b3668.
DR EnsemblBacteria; BAE77625; BAE77625; BAE77625.
DR GeneID; 66672435; -.
DR GeneID; 948195; -.
DR KEGG; ecj:JW3643; -.
DR KEGG; eco:b3668; -.
DR PATRIC; fig|511145.12.peg.3790; -.
DR EchoBASE; EB1045; -.
DR eggNOG; COG3851; Bacteria.
DR HOGENOM; CLU_041023_0_0_6; -.
DR InParanoid; P09835; -.
DR OMA; FCLWVIA; -.
DR PhylomeDB; P09835; -.
DR BioCyc; EcoCyc:UHPB-MON; -.
DR BioCyc; MetaCyc:UHPB-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P09835; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF05231; MASE1; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..500
FT /note="Signal transduction histidine-protein
FT kinase/phosphatase UhpB"
FT /id="PRO_0000074890"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:8349544"
FT DOMAIN 311..499
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 313
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11053370"
FT MUTAGEN 313
FT /note="H->E: Lack of autokinase activity."
FT /evidence="ECO:0000269|PubMed:11053370"
FT CONFLICT 337..357
FT /note="NASVKQSGQLIEQLSLGVYDA -> RRQREAERAAHRTTIAGRLRR (in
FT Ref. 1; AAA24721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56306 MW; A7353FC1F1D53152 CRC64;
MKTLFSRLIT VIACFFIFSA AWFCLWSISL HLVERPDMAV LLFPFGLRLG LMLQCPRGYW
PVLLGAEWLL IYWLTQAVGL THFPLLMIGS LLTLLPVALI SRYRHQRDWR TLLLQGAALT
AAALLQSLPW LWHGKESWNA LLLTLTGGLT LAPICLVFWH YLANNTWLPL GPSLVSQPIN
WRGRHLVWYL LLFVISLWLQ LGLPDELSRF TPFCLALPII ALAWHYGWQG ALIATLMNAI
ALIASQTWRD HPVDLLLSLL VQSLTGLLLG AGIQRLRELN QSLQKELARN QHLAERLLET
EESVRRDVAR ELHDDIGQTI TAIRTQAGIV QRLAADNASV KQSGQLIEQL SLGVYDAVRR
LLGRLRPRQL DDLTLEQAIR SLMREMELEG RGIVSHLEWR IDESALSENQ RVTLFRVCQE
GLNNIVKHAD ASAVTLQGWQ QDERLMLVIE DDGSGLPPGS GQQGFGLTGM RERVTALGGT
LHISCLHGTR VSVSLPQRYV
