QSEC_HAEIN
ID QSEC_HAEIN Reviewed; 451 AA.
AC P45336;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sensor protein QseC;
DE EC=2.7.13.3;
GN Name=qseC; OrderedLocusNames=HI_1707;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Member of a two-component regulatory system QseB/QseC. May
CC activate QseB by phosphorylation (By similarity). {ECO:0000250}.
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 ---------------------------------------------------------------------------
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; L42023; AAC23353.1; -; Genomic_DNA.
DR PIR; E64137; E64137.
DR RefSeq; NP_439849.1; NC_000907.1.
DR RefSeq; WP_005694197.1; NC_000907.1.
DR AlphaFoldDB; P45336; -.
DR SMR; P45336; -.
DR STRING; 71421.HI_1707; -.
DR EnsemblBacteria; AAC23353; AAC23353; HI_1707.
DR KEGG; hin:HI_1707; -.
DR PATRIC; fig|71421.8.peg.1786; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_000445_89_37_6; -.
DR OMA; DKLFDTQ; -.
DR PhylomeDB; P45336; -.
DR BioCyc; HINF71421:G1GJ1-1723-MON; -.
DR BRENDA; 2.7.13.3; 2529.
DR Proteomes; UP000000579; 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:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR013727; 2CSK_N.
DR InterPro; IPR003660; HAMP_dom.
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; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein 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..451
FT /note="Sensor protein QseC"
FT /id="PRO_0000074705"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..162
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 181..233
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 241..451
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 244
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 451 AA; 51271 MW; 00C86B648128D383 CRC64;
MKNRSLTLRL ISVLCLTALF VWLGSTLVAW WQVRHDVNKV FDAQQVLFAE RLANSDLSTI
LLESSTTLNK NSQSVLKKSY DDDALAFAIF SKTGKLLFSD GRNGKDFIFN YKTGFYNANI
YDDDDKWRIF WRMAANGELV IAVGQELDYR EDLIEEMILG QMWIWFASLP ILIIVLGWLI
HKELRPIKRL SQEVQTRKSG DVSLLNTEGL PVEILPLVKN LNQFFDRTSA MLQRERRFTS
DAAHELRSPL AALRIQIEVA QLAGDDVALR EQALLHLTQG IDRASQLIEQ LLTLSRLDNL
QALETLQLLD WEAIVQSLIS ERYFVAEKRK ITLVFEKESE PKQKQGQSIL VSLMLRNLLD
NAIKYCPEDT IVSVKISSSQ IIIEDNGGGV EPEDLKKLGQ RFYRPAGQNE KGSGLGLSIV
MRIAELHGFK VRLENVVKEG RRIGLKAIIS L