(data stored in ACNUC9435 zone)

HOGENOM: ECOK1_1_PE1008

ID   ECOK1_1_PE1008                       STANDARD;      PRT;   486 AA.
AC   ECOK1_1_PE1008; A1AA23;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=Sensor protein PhoQ; (ECOK1_1.PE1008).
GN   Name=phoQ; OrderedLocusNames=Ecok1_10190; ORFNames=APECO1_211;
OS   ESCHERICHIA COLI APEC O1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOK1_1.PE1008.
CC       Escherichia coli APEC O1, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:A1AA23_ECOK1
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
CC   -!- GENE_FAMILY: HOG000274481 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; A1AA23; -.
DR   EMBL; CP000468; ABJ00513.1; -; Genomic_DNA.
DR   RefSeq; YP_852227.1; NC_008563.1.
DR   ProteinModelPortal; A1AA23; -.
DR   SMR; A1AA23; 45-188, 214-481.
DR   STRING; A1AA23; -.
DR   EnsemblBacteria; EBESCT00000038493; EBESCP00000037010; EBESCG00000037543.
DR   GeneID; 4492299; -.
DR   GenomeReviews; CP000468_GR; Ecok1_10190.
DR   KEGG; ecv:APECO1_211; -.
DR   eggNOG; COG0642; -.
DR   GeneTree; EBGT00050000008662; -.
DR   OMA; AHWSLRP; -.
DR   ProtClustDB; PRK10815; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR003660; HAMP_linker_domain.
DR   InterPro; IPR015014; PhoQ_Sensor.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003661; Sig_transdc_His_kin_sub1_dim/P.
DR   InterPro; IPR005467; Sig_transdc_His_kinase_core.
DR   InterPro; IPR009082; Sig_transdc_His_kinase_dimeric.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08918; PhoQ_Sensor; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   SUPFAM; SSF47384; His_kin_homodim; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   HOGENOMDNA; ECOK1_1.PE1008; -.
KW   sensor protein PhoQ;
KW   ATP-binding; Complete proteome; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane;
KW   Two-component regulatory system.
SQ   SEQUENCE   486 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MKKLLHLFFP LSLRVRFLLA TAAVVLVLSL AYGMVALIGY SVSFDKTTFR LLRGESNLFY
     TLAKWENNKL HVELPENIDK QSPTMTLIYD ENGQLLWAQR DVPWLMKMIQ PDWLKSNGFH
     EIEADVNDTS LLLSGDHSIQ QQLQEVREDD DDAEMTHSVA VNVYPATSRM PKLTIVVVDT
     IPVELKSSYM VWSWFIYVLS ANLLLVIPLL WVAAWWSLRP IEALAKEVRE LEEHNRELLN
     PATTRELTSL VRNLNRLLKS ERERYDKYRT TLTDLTHSLK TPLAVLQSTL RSLRSEKMSV
     SDAEPVMLEQ ISRISQQIGY YLHRASMRGG TLLSRELHPV APLLDNLTSA LNKVYQRKGV
     NISLDISPEI SFVGEQNDFV EVMGNVLDNA CKYCLEFVEI SARQTDEHLY IVVEDDGPGI
     PLSKREVIFD RGQRVDTLRP GQGVGLAVAR EITEQYEGKI VAGESMLGGA RMEVIFGRQH
     SAPKDE
//

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