ENVZ_SALTS
ID ENVZ_SALTS Reviewed; 450 AA.
AC A0A0H3NIL4;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2020, sequence version 2.
DT 03-AUG-2022, entry version 29.
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=SL1344_3468;
OS Salmonella typhimurium (strain SL1344).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=216597;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL1344;
RX PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT "The transcriptional landscape and small RNAs of Salmonella enterica
RT serovar Typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN [2]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=2543631; DOI=10.1128/iai.57.7.2136-2140.1989;
RA Dorman C.J., Chatfield S., Higgins C.F., Hayward C., Dougan G.;
RT "Characterization of porin and ompR mutants of a virulent strain of
RT Salmonella typhimurium: ompR mutants are attenuated in vivo.";
RL Infect. Immun. 57:2136-2140(1989).
CC -!- FUNCTION: Member of the two-component regulatory system EnvZ/OmpR
CC involved in osmoregulation (particularly of genes ompF and ompC) as
CC well as other genes (PubMed:2543631). EnvZ functions as a membrane-
CC associated protein kinase that phosphorylates OmpR in response to
CC environmental signals; at low osmolarity OmpR activates ompF
CC transcription, while at high osmolarity it represses ompF and activates
CC ompC transcription (Probable). {ECO:0000269|PubMed:2543631,
CC ECO:0000305|PubMed:2543631}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CBW19563.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; FQ312003; CBW19563.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_001253818.1; NZ_QASL01000006.1.
DR AlphaFoldDB; A0A0H3NIL4; -.
DR SMR; A0A0H3NIL4; -.
DR EnsemblBacteria; CBW19563; CBW19563; SL1344_3468.
DR KEGG; sey:SL1344_3468; -.
DR PATRIC; fig|216597.6.peg.3862; -.
DR HOGENOM; CLU_000445_89_27_6; -.
DR Proteomes; UP000008962; 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;
KW Virulence.
FT CHAIN 1..450
FT /note="Sensor histidine kinase EnvZ"
FT /id="PRO_0000448908"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
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; 50374 MW; B3624AE0CA834FED 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 YGNGWIKVSS
GTESHRAWFQ VEDDGPGIKP EQRKHLFQPF VRGDSARSTS GTGLGLAIVQ RIIDNHNGML
EIGTSERGGL SIRAWLPVPV ARVQGTTKEA
