ENVZ_SHIFM
ID ENVZ_SHIFM Reviewed; 450 AA.
AC A0A4P7TSF2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-JUL-2019, sequence version 1.
DT 03-AUG-2022, entry version 15.
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; ORFNames=EKN05_021995;
OS Shigella flexneri serotype 5a (strain M90T).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=1086030;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M90T / Serotype 5a;
RA Cervantes-Rivera R., Puhar A.;
RT "Complete genome sequence and annotation of the laboratory reference strain
RT Shigella flexneri 5a M90T and genome-wide transcription start site
RT determination.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=2121709; DOI=10.1128/jb.172.11.6274-6281.1990;
RA Bernardini M.L., Fontaine A., Sansonetti P.J.;
RT "The two-component regulatory system ompR-envZ controls the virulence of
RT Shigella flexneri.";
RL J. Bacteriol. 172:6274-6281(1990).
RN [3]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=M90T / Serotype 5a;
RX PubMed=8359885; DOI=10.1128/iai.61.9.3625-3635.1993;
RA Bernardini M.L., Sanna M.G., Fontaine A., Sansonetti P.J.;
RT "OmpC is involved in invasion of epithelial cells by Shigella flexneri.";
RL Infect. Immun. 61:3625-3635(1993).
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). Unlike E.coli, OmpC is expressed at both low and high
CC osmolarity, while OmpF is expressed at low osmolarity. This two-
CC component system plays a role in virulence (PubMed:2121709,
CC PubMed:8359885). Virulence genes of the vir locus are up-regulated
CC within 30 minutes upon growth in high osmolarity medium
CC (PubMed:2121709). {ECO:0000250|UniProtKB:P0AEJ4,
CC ECO:0000269|PubMed:2121709, ECO:0000269|PubMed:8359885}.
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 -!- DISRUPTION PHENOTYPE: Single gene deletion invades HeLa cells poorly,
CC has a reduced ability to multiply in host cells and does not cause
CC keratoconjunctivitis in guinea pigs. A double ompR-envZ deletion
CC invades HeLa cells less well than the single mutant, has a limited
CC ability to multiply in host cells and does not cause
CC keratoconjunctivitis in guinea pigs (PubMed:2121709). A double ompR-
CC envZ deletion has a lowered rate of infection of HeLa cells. Bacteria
CC are seriously impaired in their ability to spread between host cells.
CC The double deletion strain expresses very low amounts of OmpC and no
CC OmpF (PubMed:8359885). {ECO:0000269|PubMed:2121709,
CC ECO:0000269|PubMed:8359885}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP037923; QCC33845.1; -; Genomic_DNA.
DR RefSeq; WP_001253696.1; NZ_CM001474.1.
DR AlphaFoldDB; A0A4P7TSF2; -.
DR SMR; A0A4P7TSF2; -.
DR EnsemblBacteria; QCC33845; QCC33845; EKN05_021995.
DR GeneID; 66672714; -.
DR Proteomes; UP000296678; 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 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_0000448909"
FT TRANSMEM 12..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..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; 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
