EVGS_ECOLI
ID EVGS_ECOLI Reviewed; 1197 AA.
AC P30855; P77644; Q9RF36; Q9RF37;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Sensor protein EvgS;
DE EC=2.7.13.3;
DE Flags: Precursor;
GN Name=evgS; OrderedLocusNames=b2370, JW2367;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8125343; DOI=10.1016/0378-1119(94)90733-1;
RA Utsumi R., Katayama S., Taniguchi M., Horie T., Ikeda M., Igaki S.,
RA Nakagawa H., Miwa A., Tanabe H., Noda M.;
RT "Newly identified genes involved in the signal transduction of Escherichia
RT coli K-12.";
RL Gene 140:73-77(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1289796;
RA Utsumi R., Katayama S., Ikeda M., Igaki S., Nakagawa H., Miwa A.,
RA Taniguchi M., Noda M.;
RT "Cloning and sequence analysis of the evgAS genes involved in signal
RT transduction of Escherichia coli K-12.";
RL Nucleic Acids Symp. Ser. 27:149-150(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (VARIANTS EVGS1 AND EVGS4).
RC STRAIN=K12;
RX PubMed=10923791; DOI=10.1271/bbb.64.1203;
RA Kato A., Ohnishi H., Yamamoto K., Furuta E., Tanabe H., Utsumi R.;
RT "Transcription of emrKY is regulated by the EvgA-EvgS two-component system
RT in Escherichia coli K-12.";
RL Biosci. Biotechnol. Biochem. 64:1203-1209(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [5]
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 [6]
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 [7]
RP CHARACTERIZATION.
RX PubMed=9535079; DOI=10.1046/j.1365-2958.1998.00716.x;
RA Perraud A.-L., Kimmel B., Weiss V., Gross R.;
RT "Specificity of the BvgAS and EvgAS phosphorelay is mediated by the C-
RT terminal HPt domains of the sensor proteins.";
RL Mol. Microbiol. 27:875-887(1998).
CC -!- FUNCTION: Member of the two-component regulatory system EvgS/EvgA.
CC Phosphorylates EvgA via a four-step phosphorelay in response to
CC environmental signals.
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:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- PTM: Activation requires a sequential transfer of a phosphate group
CC from a His in the primary transmitter domain, to an Asp in the receiver
CC domain and to a His in the secondary transmitter domain.
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DR EMBL; D14008; BAA03108.1; -; Genomic_DNA.
DR EMBL; AF201840; AAF17563.1; -; Genomic_DNA.
DR EMBL; AF201841; AAF17564.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75429.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16241.1; -; Genomic_DNA.
DR PIR; G65010; G65010.
DR RefSeq; NP_416871.1; NC_000913.3.
DR RefSeq; WP_001326970.1; NZ_LN832404.1.
DR AlphaFoldDB; P30855; -.
DR SMR; P30855; -.
DR BioGRID; 4260559; 16.
DR BioGRID; 851185; 1.
DR DIP; DIP-9545N; -.
DR IntAct; P30855; 5.
DR STRING; 511145.b2370; -.
DR jPOST; P30855; -.
DR PaxDb; P30855; -.
DR PRIDE; P30855; -.
DR EnsemblBacteria; AAC75429; AAC75429; b2370.
DR EnsemblBacteria; BAA16241; BAA16241; BAA16241.
DR GeneID; 946844; -.
DR KEGG; ecj:JW2367; -.
DR KEGG; eco:b2370; -.
DR PATRIC; fig|1411691.4.peg.4359; -.
DR EchoBASE; EB1567; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_6; -.
DR InParanoid; P30855; -.
DR OMA; NFGKHEA; -.
DR PhylomeDB; P30855; -.
DR BioCyc; EcoCyc:EVGS-MON; -.
DR BioCyc; MetaCyc:EVGS-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P30855; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; ISM:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; ISM: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:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0010447; P:response to acidic pH; IDA:EcoCyc.
DR GO; GO:0010038; P:response to metal ion; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 1.20.120.160; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00497; SBP_bac_3; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00062; PBPb; 2.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF47226; SSF47226; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Signal;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..1197
FT /note="Sensor protein EvgS"
FT /id="PRO_0000032371"
FT TOPO_DOM 22..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..537
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..1197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 718..938
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT DOMAIN 960..1074
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DOMAIN 1098..1197
FT /note="HPt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT MOD_RES 721
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 1009
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 1137
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00110"
FT VARIANT 577
FT /note="F -> S (in EvgS1; constitutively active)"
FT VARIANT 701
FT /note="E -> G (in EvgS4; constitutively active)"
FT CONFLICT 152
FT /note="L -> F (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 242..243
FT /note="FF -> PL (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 275
FT /note="W -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 420..421
FT /note="SQ -> FE (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="G -> D (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 758
FT /note="G -> K (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 761
FT /note="L -> V (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="S -> L (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1045
FT /note="R -> H (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 1074
FT /note="H -> Y (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1197 AA; 134743 MW; E8E1DE0F797B1278 CRC64;
MKFLPYIFLL CCGLWSTISF ADEDYIEYRG ISSNNRVTLD PLRLSNKELR WLASKKNLVI
AVHKSQTATL LHTDSQQRVR GINADYLNLL KRALNIKLTL REYADHQKAM DALAEGEVDI
VLSHLVTSPP LNNDIAATKP LIITFPALVT TLHDSMRPLT SPKPVNIARV ANYPPDEVIH
QSFPKATIIS FTNLYQALAS VSAGHNDYFI GSNIITSSMI SRYFTHSLNV VKYYNSPRQY
NFFLTRKESV ILNEVLNRFV DALTNEVRYE VSQNWLDTGN LAFLNKPLEL TEHEKQWIKQ
HPNLKVLENP YSPPYSMTDE NGSVRGVMGD ILNIITLQTG LNFSPITVSH NIHAGTQLSP
GGWDIIPGAI YSEDRENNVL FAEAFITTPY VFVMQKAPDS EQTLKKGMKV AIPYYYELHS
QLKEMYPEVE WIQVDNASAA FHKVKEGELD ALVATQLNSR YMIDHYYPNE LYHFLIPGVP
NASLSFAFPR GEPELKDIIN KALNAIPPSE VLRLTEKWIK MPNVTIDTWD LYSEQFYIVT
TLSVLLVGSS LLWGFYLLRS VRRRKVIQGD LENQISFRKA LSDSLPNPTY VVNWQGNVIS
HNSAFEHYFT ADYYKNAMLP LENSDSPFKD VFSNAHEVTA ETKENRTIYT QVFEIDNGIE
KRCINHWHTL CNLPASDNAV YICGWQDITE TRDLINALEV EKNKAIKATV AKSQFLATMS
HEIRTPISSI MGFLELLSGS GLSKEQRVEA ISLAYATGQS LLGLIGEILD VDKIESGNYQ
LQPQWVDIPT LVQNTCHSFG AIAASKSIAL SCSSTFPEHY LVKIDPQAFK QVLSNLLSNA
LKFTTEGAVK ITTSLGHIDD NHAVIKMTIM DSGSGLSQEE QQQLFKRYSQ TSAGRQQTGS
GLGLMICKEL IKNMQGDLSL ESHPGIGTTF TITIPVEISQ QVATVEAKAE QPITLPEKLS
ILIADDHPTN RLLLKRQLNL LGYDVDEATD GVQALHKVSM QHYDLLITDV NMPNMDGFEL
TRKLREQNSS LPIWGLTANA QANEREKGLS CGMNLCLFKP LTLDVLKTHL SQLHQVAHIA
PQYRHLDIEA LKNNTANDLQ LMQEILMTFQ HETHKDLPAA FQALEAGDNR TFHQCIHRIH
GAANILNLQK LINISHQLEI TPVSDDSKPE ILQLLNSVKE HIAELDQEIA VFCQKND
