ENVZ_SALTI
ID ENVZ_SALTI Reviewed; 450 AA.
AC P41406;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sensor histidine kinase EnvZ {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P0AEJ4};
DE AltName: Full=Osmolarity sensor protein EnvZ {ECO:0000305};
GN Name=envZ; OrderedLocusNames=STY4295, t4005;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMSS-1;
RA Martinez-Flores I., Bustamante V., Puente J.L., Calva E.;
RT "Cloning and characterization of the Salmonella typhi ompR and envZ
RT genes.";
RL Asia Pac. J. Mol. Biol. Biotechnol. 3:135-144(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 700931 / Ty2 / CVD 908;
RX PubMed=8063417; DOI=10.1128/iai.62.9.3984-3993.1994;
RA Pickard D.J., Li J., Roberts M.R., Maskell D., Hone D., Levine M.,
RA Dougan G., Chatfield S.;
RT "Characterization of defined ompR mutants of Salmonella typhi: ompR is
RT involved in the regulation of Vi polysaccharide expression.";
RL Infect. Immun. 62:3984-3993(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Member of the two-component regulatory system EnvZ/OmpR
CC involved in regulating expression of the outer membrane porins OmpC and
CC OmpF as well as other genes. Unlike E.coli or S.typhimurium both porins
CC are expressed constitutively. Involved in regulation of the
CC biosynthesis of Vi polysaccharide, a capsular antigen thought to be
CC involved in the virulence of S.typhi. Vi antigen is synthesized at low
CC NaCl concentrations (under 0.4 M) (PubMed:8063417). EnvZ functions as a
CC membrane-associated protein kinase that phosphorylates OmpR in response
CC to environmental signals (By similarity).
CC {ECO:0000250|UniProtKB:P0AEJ4, ECO:0000269|PubMed:8063417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P0AEJ4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0AEJ4}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AEJ4}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: Has several major domains; the N-terminal cytoplasmic domain is
CC followed by 2 transmembrane helices that anchor the protein in the
CC membrane; the periplasmic domain between the helices interacts with
CC MrzA. The cytoplasmic C-terminal domain has a HAMP domain joined by a
CC flexible linker to a histidine kinase domain. The HAMP domain by itself
CC is intrinsically disordered. The cytoplasmic dimerization domain (CDD)
CC forms an osmosensitive core and includes the autophosphorylated
CC histidine residue. {ECO:0000250|UniProtKB:P0AEJ4}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P0AEJ4}.
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DR EMBL; X77305; CAA54511.1; -; Genomic_DNA.
DR EMBL; X78270; CAA55077.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD08113.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71475.1; -; Genomic_DNA.
DR PIR; S41888; S41888.
DR RefSeq; NP_458403.1; NC_003198.1.
DR RefSeq; WP_001253815.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; P41406; -.
DR SMR; P41406; -.
DR STRING; 220341.16505092; -.
DR EnsemblBacteria; AAO71475; AAO71475; t4005.
DR KEGG; stt:t4005; -.
DR KEGG; sty:STY4295; -.
DR PATRIC; fig|220341.7.peg.4389; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_27_6; -.
DR OMA; WIRPPQA; -.
DR BRENDA; 2.7.13.3; 5557.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 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; 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; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Stress response; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..450
FT /note="Sensor histidine kinase EnvZ"
FT /id="PRO_0000074760"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 36..158
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 180..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 180..232
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 240..440
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT REGION 223..289
FT /note="Cytoplasmic dimerization domain (CDD), when
FT dimerized forms osmosensitive core"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4"
FT BINDING 347..351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4"
FT BINDING 373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4"
FT BINDING 392..393
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4"
FT BINDING 402..406
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4"
FT MOD_RES 243
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0AEJ4,
FT ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 450 AA; 50420 MW; B5C88C4CA045E52D CRC64;
MRRMRFSPRS SFARTLLLIV TLLFVSLVTT YLVVLNFAIL PSLQQFNKVL AYEVRMLMTD
KLQLEDGTQL VVPPAFRREI YRELGISLYT NEAAEEAGLR WAQHYEFLSH QMAQQLGGPT
EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR
IQNRPLVDLE HAALQVGKGI IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG
VSHDLRTPLT RIRLATEMMG EEDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD
LNSVLGEVIA AESGYEREIN TALQAGSIQV KMHPLSIKRA VANMVVNAAR YGNCWIKVSS
GTESHRAWFQ VEDDGPGIKP EQRKHLFQPF VRGDSARSTS GTGLGLAIVQ RIIDNHNGML
EIGTSERGGL SIRAWLPVPV ARVQGTTKEA
