QSEC_ECOLI
ID QSEC_ECOLI Reviewed; 449 AA.
AC P40719; Q2M9H4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Sensor protein QseC;
DE EC=2.7.13.3;
GN Name=qseC; Synonyms=ygiY; OrderedLocusNames=b3026, JW2994;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 317-449.
RA Chatterjee P.K., Sternberg N.L.;
RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RC STRAIN=K12, and O157:H7;
RX PubMed=11929534; DOI=10.1046/j.1365-2958.2002.02803.x;
RA Sperandio V., Torres A.G., Kaper J.B.;
RT "Quorum sensing Escherichia coli regulators B and C (QseBC): a novel two-
RT component regulatory system involved in the regulation of flagella and
RT motility by quorum sensing in E. coli.";
RL Mol. Microbiol. 43:809-821(2002).
RN [5]
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).
RN [6]
RP INDUCTION BY AI-2 AND MQSR.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290, K12 / DH5-alpha, and
RC K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16352847; DOI=10.1128/jb.188.1.305-316.2006;
RA Gonzalez Barrios A.F., Zuo R., Hashimoto Y., Yang L., Bentley W.E.,
RA Wood T.K.;
RT "Autoinducer 2 controls biofilm formation in Escherichia coli through a
RT novel motility quorum-sensing regulator (MqsR, B3022).";
RL J. Bacteriol. 188:305-316(2006).
CC -!- FUNCTION: Member of a two-component regulatory system QseB/QseC.
CC Activates the flagella regulon by activating transcription of FlhDC.
CC May activate QseB by phosphorylation. {ECO:0000269|PubMed:11929534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By the signal autoinducer AI-2, through MqsR.
CC {ECO:0000269|PubMed:16352847}.
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DR EMBL; U28377; AAA69194.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76062.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77082.1; -; Genomic_DNA.
DR EMBL; U18656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; H65089; H65089.
DR RefSeq; NP_417498.1; NC_000913.3.
DR RefSeq; WP_000673402.1; NZ_SSZK01000023.1.
DR PDB; 2KSE; NMR; -; A=2-185.
DR PDB; 3JZ3; X-ray; 2.50 A; A/B=236-449.
DR PDBsum; 2KSE; -.
DR PDBsum; 3JZ3; -.
DR AlphaFoldDB; P40719; -.
DR SMR; P40719; -.
DR BioGRID; 4259459; 16.
DR IntAct; P40719; 6.
DR STRING; 511145.b3026; -.
DR PaxDb; P40719; -.
DR PRIDE; P40719; -.
DR EnsemblBacteria; AAC76062; AAC76062; b3026.
DR EnsemblBacteria; BAE77082; BAE77082; BAE77082.
DR GeneID; 947174; -.
DR KEGG; ecj:JW2994; -.
DR KEGG; eco:b3026; -.
DR PATRIC; fig|1411691.4.peg.3704; -.
DR EchoBASE; EB2845; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_000445_89_37_6; -.
DR InParanoid; P40719; -.
DR OMA; DKLFDTQ; -.
DR PhylomeDB; P40719; -.
DR BioCyc; EcoCyc:EG12658-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR EvolutionaryTrace; P40719; -.
DR PHI-base; PHI:6890; -.
DR PRO; PR:P40719; -.
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; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0090593; P:peptidyl-histidine autophosphorylation; ISM:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:2000145; P:regulation of cell motility; IMP:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR DisProt; DP00774; -.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR013727; 2CSK_N.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF08521; 2CSK_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..449
FT /note="Sensor protein QseC"
FT /id="PRO_0000074703"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..156
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 243..449
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 246
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:2KSE"
FT HELIX 14..32
FT /evidence="ECO:0007829|PDB:2KSE"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2KSE"
FT HELIX 159..182
FT /evidence="ECO:0007829|PDB:2KSE"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3JZ3"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:3JZ3"
FT HELIX 350..366
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3JZ3"
FT HELIX 419..428
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:3JZ3"
FT STRAND 441..448
FT /evidence="ECO:0007829|PDB:3JZ3"
SQ SEQUENCE 449 AA; 50282 MW; 9F00CB507FDFA715 CRC64;
MKFTQRLSLR VRLTLIFLIL ASVTWLLSSF VAWKQTTDNV DELFDTQLML FAKRLSTLDL
NEINAADRMA QTPNRLKHGH VDDDALTFAI FTHDGRMVLN DGDNGEDIPY SYQREGFADG
QLVGEDDPWR FVWMTSPDGK YRIVVGQEWE YREDMALAIV AGQLIPWLVA LPIMLIIMMV
LLGRELAPLN KLALALRMRD PDSEKPLNAT GVPSEVRPLV ESLNQLFART HAMMVRERRF
TSDAAHELRS PLTALKVQTE VAQLSDDDPQ ARKKALLQLH SGIDRATRLV DQLLTLSRLD
SLDNLQDVAE IPLEDLLQSS VMDIYHTAQQ AKIDVRLTLN AHSIKRTGQP LLLSLLVRNL
LDNAVRYSPQ GSVVDVTLNA DNFIVRDNGP GVTPEALARI GERFYRPPGQ TATGSGLGLS
IVQRIAKLHG MNVEFGNAEQ GGFEAKVSW
