ID   CREC_ECOLI              Reviewed;         474 AA.
AC   P08401; Q2M5R8;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   16-JUN-2009, entry version 99.
DE   RecName: Full=Sensor protein creC;
DE            EC=2.7.13.3;
GN   Name=creC; Synonyms=phoM; OrderedLocusNames=b4399, JW4362;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87008393; PubMed=3531171;
RA   Amemura M., Makino K., Shinagawa H., Nakata A.;
RT   "Nucleotide sequence of the phoM region of Escherichia coli: four open
RT   reading frames may constitute an operon.";
RL   J. Bacteriol. 168:294-302(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=95334362; PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; 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.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
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
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-474.
RC   STRAIN=K12;
RX   MEDLINE=88216172; PubMed=2835585;
RX   DOI=10.1111/j.1365-2958.1988.tb00012.x;
RA   Drury L.S., Buxton R.S.;
RT   "Identification and sequencing of the Escherichia coli cet gene which
RT   codes for an inner membrane protein, mutation of which causes
RT   tolerance to colicin E2.";
RL   Mol. Microbiol. 2:109-119(1988).
RN   [6]
RP   FUNCTION.
RX   MEDLINE=91035239; PubMed=2228961;
RA   Amemura M., Makino K., Shinagawa H., Nakata A.;
RT   "Cross talk to the phosphate regulon of Escherichia coli by PhoM
RT   protein: PhoM is a histidine protein kinase and catalyzes
RT   phosphorylation of PhoB and PhoM-open reading frame 2.";
RL   J. Bacteriol. 172:6300-6307(1990).
RN   [7]
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).
CC   -!- FUNCTION: Member of the two-component regulatory system creC/creB
CC       involved in catabolic regulation. CreC may function as a membrane-
CC       associated protein kinase that phosphorylates creB in response to
CC       environmental signals. CreC can also phosphorylate phoB.
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Contains 1 HAMP domain.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
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DR   EMBL; M13608; AAA24375.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97295.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77352.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78388.1; -; Genomic_DNA.
DR   EMBL; Y00538; CAA68601.1; -; Genomic_DNA.
DR   PIR; S56623; RGECFM.
DR   RefSeq; AP_004887.1; -.
DR   RefSeq; NP_418816.1; -.
DR   DIP; DIP:9319N; -.
DR   GeneID; 948609; -.
DR   GenomeReviews; AP009048_GR; JW4362.
DR   GenomeReviews; U00096_GR; b4399.
DR   KEGG; ecj:JW4362; -.
DR   KEGG; eco:b4399; -.
DR   EchoBASE; EB0723; -.
DR   EcoGene; EG10730; creC.
DR   HOGENOM; P08401; -.
DR   OMA; P08401; RIFLVYF.
DR   BioCyc; EcoCyc:CREC-MON; -.
DR   BRENDA; 2.7.13.3; 246.
DR   GO; GO:0016021; C:integral to 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:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro.
DR   GO; GO:0000160; P:two-component signal transduction system (p...; IEA:UniProtKB-KW.
DR   InterPro; IPR003594; ATP_bd_ATPase.
DR   InterPro; IPR003660; HAMP_linker_domain.
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   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; Complete proteome;
KW   Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Transmembrane; Two-component regulatory system.
FT   CHAIN         1    474       Sensor protein creC.
FT                                /FTId=PRO_0000074742.
FT   TOPO_DOM      1      6       Periplasmic (Potential).
FT   TRANSMEM      7     27       Potential.
FT   TOPO_DOM     28    146       Cytoplasmic (Potential).
FT   TRANSMEM    147    167       Potential.
FT   TOPO_DOM    168    183       Periplasmic (Potential).
FT   TRANSMEM    184    204       Potential.
FT   TOPO_DOM    205    474       Cytoplasmic (Potential).
FT   DOMAIN      205    255       HAMP.
FT   DOMAIN      262    473       Histidine kinase.
FT   MOD_RES     265    265       Phosphohistidine; by autocatalysis (By
FT                                similarity).
FT   CONFLICT     77     77       R -> P (in Ref. 1; AAA24375).
SQ   SEQUENCE   474 AA;  52176 MW;  9CEB8CCE406E3163 CRC64;
     MRIGMRLLLG YFLLVAVAAW FVLAIFVKEV KPGVRRATEG TLIDTATLLA ELARPDLLSG
     DPTHGQLAQA FNQLQHRPFR ANIGGINKVR NEYHVYMTDA QGKVLFDSAN KAVGQDYSRW
     NDVWLTLRGQ YGARSTLQNP ADPESSVMYV AAPIMDGSRL IGVLSVGKPN AAMAPVIKRS
     ERRILWASAI LLGIALVIGA GMVWWINRSI ARLTRYADSV TDNKPVPLPD LGSSELRKLA
     QALESMRVKL EGKNYIEQYV YALTHELKSP LAAIRGAAEI LREGPPPEVV ARFTDNILTQ
     NARMQALVET LLRQARLENR QEVVLTAVDV AALFRRVSEA RTVQLAEKKI TLHVTPTEVN
     VAAEPALLEQ ALGNLLDNAI DFTPESGCIT LSAEVDQEHV TLKVLDTGSG IPDYALSRIF
     ERFYSLPRAN GQKSSGLGLA FVSEVARLFN GEVTLRNVQE GGVLASLRLH RHFT
//