QSEC_ECO57
ID QSEC_ECO57 Reviewed; 449 AA.
AC Q8X524; Q8X2K3; Q8X2K4;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Sensor protein QseC;
DE EC=2.7.13.3;
GN Name=qseC; OrderedLocusNames=Z4378, ECs3908/ECs3909;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP FUNCTION.
RC STRAIN=K12, and O157:H7 / EHEC;
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).
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 {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: By the AI-2 quorum sensing system.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB37332.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58160.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37331.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BA000007; BAB37332.1; ALT_FRAME; Genomic_DNA.
DR PIR; D85962; D85962.
DR PIR; D91117; D91117.
DR PIR; E91117; E91117.
DR RefSeq; WP_000673362.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X524; -.
DR SMR; Q8X524; -.
DR STRING; 155864.EDL933_4247; -.
DR EnsemblBacteria; AAG58160; AAG58160; Z4378.
DR EnsemblBacteria; BAB37331; BAB37331; ECs_3908.
DR KEGG; ece:Z4378; -.
DR PATRIC; fig|83334.175.peg.2423; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_147058_0_0_6; -.
DR OMA; DKLFDTQ; -.
DR BRENDA; 2.7.13.3; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
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 2: Evidence at transcript level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..449
FT /note="Sensor protein QseC"
FT /id="PRO_0000074704"
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"
SQ SEQUENCE 449 AA; 50259 MW; 5A2928F6ABB0BB35 CRC64;
MKFTQRLSLR VRLTLIFLIL ASVTWLLSSF VAWKQTTDNV DELFDTQLML FAKRLSTLDL
NEINAADRMA QTPNKLKHGH VDDDALTFAI FTHDGRMVLN DGDNGEDIPY SYQREGFADG
QLVGDKDQWR FVWMTSPDGK YRIVVGQEWE YREDMALAIV AGQLIPWLVA LPVMLIIMMV
LLGRELAPLN KLALALRMRD PDSEKPLNAT GVPSEVRPLV ESLNQLFART HAMMVRERRF
TSDAAHELRS PLTALKVQTE VAQLSDDDPQ ARKKALLQLH SGIDRATRLV DQLLTLSRLD
SLDNLQDVAE IPLEDLLQSS VMDIYHTAQQ AKIDVRLTLN VQGIKRTGQP LLLSLLVRNL
LDNAVRYSPQ GSVVDVTLNA DNFIVRDNGP GVTPEALARI GERFYRPPGQ TATGSGLGLS
IVQRIAKLHG MNVEFGNAEQ GGFEAKVSW
