CREC_ECOLI
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 03-AUG-2022, entry version 194.
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; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3531171; DOI=10.1128/jb.168.1.294-302.1986;
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 PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT 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 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 [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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-474.
RC STRAIN=K12;
RX PubMed=2835585; 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 codes
RT for an inner membrane protein, mutation of which causes tolerance to
RT colicin E2.";
RL Mol. Microbiol. 2:109-119(1988).
RN [6]
RP FUNCTION.
RX PubMed=2228961; DOI=10.1128/jb.172.11.6300-6307.1990;
RA Amemura M., Makino K., Shinagawa H., Nakata A.;
RT "Cross talk to the phosphate regulon of Escherichia coli by PhoM protein:
RT PhoM is a histidine protein kinase and catalyzes phosphorylation of PhoB
RT and PhoM-open reading frame 2.";
RL J. Bacteriol. 172:6300-6307(1990).
RN [7]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
RN [8]
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 {ECO:0000269|PubMed:15522865, ECO:0000269|PubMed:2228961}.
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 -!- PTM: Autophosphorylated.
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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; NP_418816.1; NC_000913.3.
DR RefSeq; WP_001219559.1; NZ_LN832404.1.
DR RefSeq; WP_001219577.1; NZ_CP064683.1.
DR AlphaFoldDB; P08401; -.
DR SMR; P08401; -.
DR BioGRID; 4261905; 10.
DR BioGRID; 852902; 1.
DR DIP; DIP-9319N; -.
DR IntAct; P08401; 5.
DR STRING; 511145.b4399; -.
DR PaxDb; P08401; -.
DR PRIDE; P08401; -.
DR EnsemblBacteria; AAC77352; AAC77352; b4399.
DR EnsemblBacteria; BAE78388; BAE78388; BAE78388.
DR GeneID; 948609; -.
DR KEGG; ecj:JW4362; -.
DR KEGG; eco:b4399; -.
DR PATRIC; fig|511145.12.peg.4548; -.
DR EchoBASE; EB0723; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_31_6; -.
DR InParanoid; P08401; -.
DR OMA; RWNDVYL; -.
DR PhylomeDB; P08401; -.
DR BioCyc; EcoCyc:CREC-MON; -.
DR BioCyc; MetaCyc:CREC-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P08401; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0019660; P:glycolytic fermentation; IEP:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
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; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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 SUPFAM; SSF103190; SSF103190; 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..474
FT /note="Sensor protein CreC"
FT /id="PRO_0000074742"
FT TOPO_DOM 1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..146
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..183
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 205..255
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 262..473
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 265
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 77
FT /note="R -> P (in Ref. 1; AAA24375)"
FT /evidence="ECO:0000305"
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
