EVGS_ECO57
ID EVGS_ECO57 Reviewed; 1197 AA.
AC P58402;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sensor protein EvgS;
DE EC=2.7.13.3;
DE Flags: Precursor;
GN Name=evgS; OrderedLocusNames=Z3632, ECs3249;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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 (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: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. {ECO:0000250}.
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DR EMBL; AE005174; AAG57495.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36672.1; -; Genomic_DNA.
DR PIR; A91035; A91035.
DR PIR; C85879; C85879.
DR RefSeq; NP_311276.1; NC_002695.1.
DR RefSeq; WP_001301578.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58402; -.
DR SMR; P58402; -.
DR STRING; 155864.EDL933_3538; -.
DR PRIDE; P58402; -.
DR EnsemblBacteria; AAG57495; AAG57495; Z3632.
DR EnsemblBacteria; BAB36672; BAB36672; ECs_3249.
DR GeneID; 915650; -.
DR KEGG; ece:Z3632; -.
DR KEGG; ecs:ECs_3249; -.
DR PATRIC; fig|386585.9.peg.3393; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG0834; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_37_3_6; -.
DR OMA; NFGKHEA; -.
DR BRENDA; 2.7.13.3; 2026.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of 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:phosphorelay sensor kinase activity; IEA:InterPro.
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; 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 3: Inferred from homology;
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_0000032372"
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"
SQ SEQUENCE 1197 AA; 134954 MW; A01055089D9618E2 CRC64;
MKFLPYIFLL CCGLWSTISF ADEDYIEYRG ISSNNRVTLD PLRLSNKELR WLASKKNLVI
AVHKSQTATL LHTDSQQRVR GINADYLNLL KRALNIKLTL REYADHQKAM DALEEGEVDI
VLSHLVASPP LNDDIAATKP LIITFPALVT TLHDSMRPLT SSKPVNIARV ANYPPDEVIH
QSFPKATIIS FTNLYQALAS VSAGQNDYFI GSNIITSSMI SRYFTHSLNV VKYYNSPRQY
NFFLTRKESV ILNEVLNRFV DALTNEVRYE VSQNWLDTGN LAFLNKPLEL TEHEKQWIKQ
HPDLKVLENP YSPPYSMTDE NGSVRGVMGD ILNIITLQTG LNFSPITVSH NIHAGTQLNP
GGWDILPGAI YSEDRENNVL FAEAFITTPY VFVMQKAPDS EQTLKKGMKV AIPYYYELHS
QLKEMYPEVE WIKVDNASAA FHKVKEGELD ALVATQLNSR YMIDHYYPNE LYHFLIPGVP
NASLSFAFPR GEPELKDIIN KALNAIPPSE VLRLTEKWIK MPNVTIDTWD LYSEQFYIVT
TLSVLLVGSS LLWGFYLLRS VRRRKVIQGD LENQISFRKA LSDSLPNPTY VVNWQGNVIS
HNSAFEHYFT ADYYKNAMLP LENSESPFKD VFSNTHEVTA ETKENRTIYT QVFEIDNGIE
KRCINHWHTL CNLPASEHAV YICGWQDITE TRDLIHALEV ERNKAINATV AKSQFLATMS
HEIRTPISSI MGFLELLSGS GLSKEQRVEA ISLAYATGQS LLGLIGEILD VDKIESGNYQ
LQPQWVDIPT LVQNTCHSFG AIAASKSIAL SCSSTFPDHY LVKIDPQAFK QVLSNLLSNA
LKFTTEGAVK ITTSLVHIDD NHAVIKMTIM DSGSGLSQEE QQQLFKRYSQ TSAGRQQTGS
GLGLMICKEL IKNMQGDLSL ESHPGIGTTF TITIPVEIIQ QVAAVEAKAE QPITLPEKLS
ILIADDHPTN RLLLKRQLNL LGYDVDEATD GVQALHKVSM QHYDLLITDV NMPNVDGFEL
TRKLREQNSS LPIWGLTANA QANEREKGLN CGMNLCLFKP LTLDVLKTHL SQLHQVAHIV
PQYRHLDIEA LKNNTANDLQ LMQEILMTFQ HETHKDLPAA FHALEAGDNR TFHQCIHRIH
GAANILNLQK LINISHQLEI TPVSDDSKPE ILQLLNSVKE HIAELDQEIA VFCQQNN
