ENVZ_SHIFL
ID ENVZ_SHIFL Reviewed; 450 AA.
AC P0AEJ5; P02933;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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 EnzV {ECO:0000305};
GN Name=envZ; OrderedLocusNames=SF3423, S4340;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Weber A., Jung K.;
RT "Nucleotide sequence of the ompB operon of Shigella flexneri.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Member of the two-component regulatory system EnvZ/OmpR
CC involved in the regulation of osmoregulation (genes ompF and ompC).
CC EnvZ functions as a membrane-associated protein kinase that
CC phosphorylates OmpR in response to environmental signals (By
CC similarity). This two-component system plays a role in virulence (By
CC similarity). {ECO:0000250|UniProtKB:A0A4P7TSF2,
CC ECO:0000250|UniProtKB:P0AEJ4}.
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; AJ288905; CAC34269.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN44884.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19295.1; -; Genomic_DNA.
DR RefSeq; NP_709177.1; NC_004337.2.
DR RefSeq; WP_001253696.1; NZ_WPGW01000003.1.
DR PDB; 2LFR; NMR; -; A/B=228-289.
DR PDB; 2LFS; NMR; -; A/B=228-289.
DR PDBsum; 2LFR; -.
DR PDBsum; 2LFS; -.
DR AlphaFoldDB; P0AEJ5; -.
DR SMR; P0AEJ5; -.
DR STRING; 198214.SF3423; -.
DR EnsemblBacteria; AAN44884; AAN44884; SF3423.
DR EnsemblBacteria; AAP19295; AAP19295; S4340.
DR GeneID; 1026481; -.
DR GeneID; 66672714; -.
DR KEGG; sfl:SF3423; -.
DR KEGG; sfx:S4340; -.
DR PATRIC; fig|198214.7.peg.4039; -.
DR HOGENOM; CLU_000445_89_27_6; -.
DR OMA; WIRPPQA; -.
DR OrthoDB; 1031685at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell inner membrane; Cell membrane; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Stress response; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system; Virulence.
FT CHAIN 1..450
FT /note="Sensor histidine kinase EnvZ"
FT /id="PRO_0000074762"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 36..158
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 180..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
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"
FT HELIX 229..258
FT /evidence="ECO:0007829|PDB:2LFR"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:2LFR"
FT HELIX 264..287
FT /evidence="ECO:0007829|PDB:2LFR"
SQ SEQUENCE 450 AA; 50334 MW; D58444D038722146 CRC64;
MRRLRFSPRS SFARTLLLIV TLLFASLVTT YLVVLNFAIL PSLQQFNKVL AYEVRMLMTD
KLQLEDGTQL VVPPAFRREI YRELGISLYS NEAAEEAGLR WAQHYEFLSH QMAQQLGGPT
EVRVEVNKSS PVVWLKTWLS PNIWVRVPLT EIHQGDFSPL FRYTLAIMLL AIGGAWLFIR
IQNRPLVDLE HAALQVGKGI IPPPLREYGA SEVRSVTRAF NHMAAGVKQL ADDRTLLMAG
VSHDLRTPLT RIRLATEMMS EQDGYLAESI NKDIEECNAI IEQFIDYLRT GQEMPMEMAD
LNAVLGEVIA AESGYEREIE TALYPGSIEV KMHPLSIKRA VANMVVNAAR YGNGWIKVSS
GTEPNRAWFQ VEDDGPGIAP EQRKHLFQPF VRGDSARTIS GTGLGLAIVQ RIVDNHNGML
ELGTSERGGL SIRAWLPVPV TRAQGTTKEG
