CHEZ_HELPY
ID CHEZ_HELPY Reviewed; 253 AA.
AC O24976;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Protein phosphatase CheZ {ECO:0000303|PubMed:20497335};
DE EC=3.1.3.- {ECO:0000269|PubMed:20497335};
DE AltName: Full=Chemotaxis protein CheZ;
GN Name=cheZ {ECO:0000303|PubMed:20497335}; OrderedLocusNames=HP_0170;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-189 AND GLN-193.
RX PubMed=20497335; DOI=10.1111/j.1365-2958.2010.07200.x;
RA Lertsethtakarn P., Ottemann K.M.;
RT "A remote CheZ orthologue retains phosphatase function.";
RL Mol. Microbiol. 77:225-235(2010).
RN [3]
RP FUNCTION, INTERACTION WITH CHEPEP, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP ASP-189 AND GLN-193.
RC STRAIN=G27;
RX PubMed=26061894; DOI=10.1111/mmi.13086;
RA Lertsethtakarn P., Howitt M.R., Castellon J., Amieva M.R., Ottemann K.M.;
RT "Helicobacter pylori CheZ(HP) and ChePep form a novel chemotaxis-regulatory
RT complex distinct from the core chemotaxis signaling proteins and the
RT flagellar motor.";
RL Mol. Microbiol. 97:1063-1078(2015).
CC -!- FUNCTION: Plays an important role in bacterial chemotaxis signal
CC transduction pathway by accelerating the dephosphorylation of
CC phosphorylated CheY (CheY-P). Dephosphorylates also CheV2 but not CheV1
CC or CheV3 (PubMed:20497335). In addition, forms a distinct chemotaxis
CC regulatory complex with ChePep independently of the core chemotaxis
CC signaling proteins (PubMed:26061894). {ECO:0000269|PubMed:20497335,
CC ECO:0000269|PubMed:26061894}.
CC -!- SUBUNIT: Interacts with ChePep; this interaction is essential for each
CC other polar localization. {ECO:0000269|PubMed:26061894}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26061894}.
CC Note=Localizes to the cell poles. {ECO:0000269|PubMed:26061894}.
CC -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07242.1; -; Genomic_DNA.
DR PIR; B64541; B64541.
DR RefSeq; NP_206969.1; NC_000915.1.
DR RefSeq; WP_000191026.1; NC_018939.1.
DR AlphaFoldDB; O24976; -.
DR DIP; DIP-3127N; -.
DR IntAct; O24976; 1.
DR MINT; O24976; -.
DR STRING; 85962.C694_00840; -.
DR PaxDb; O24976; -.
DR EnsemblBacteria; AAD07242; AAD07242; HP_0170.
DR KEGG; hpy:HP_0170; -.
DR PATRIC; fig|85962.47.peg.183; -.
DR eggNOG; ENOG50338G0; Bacteria.
DR OMA; QYMNSLF; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..253
FT /note="Protein phosphatase CheZ"
FT /id="PRO_0000448752"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 189
FT /note="D->N: Complete loss of phosphatase activity.
FT Migrates poorly through the soft agar."
FT /evidence="ECO:0000269|PubMed:20497335,
FT ECO:0000269|PubMed:26061894"
FT MUTAGEN 193
FT /note="Q->R: Complete loss of phosphatase activity.
FT Migrates poorly through the soft agar."
FT /evidence="ECO:0000269|PubMed:20497335,
FT ECO:0000269|PubMed:26061894"
SQ SEQUENCE 253 AA; 28622 MW; E8E602D002F8FBFF CRC64;
MTQEELDALM NGGDLENLEA LETKEETKEE AKEEAKEEAK EEAKEKEEIK EESSSQKMTV
KKEDAEKYGK ISPNEWPPPP PTEEHKVVHQ LDDVTRDSEV KATQIFDQLD LIGASAEKIA
KMVKKIQEPL QKHQEIFDNL HGHFPHVESF KTALNEQQEI LNALKSIEEE AANCSDSSMQ
AMDIMQFQDI HRQKIERVVN VMRALSQYMN SLFEGKIDDS KRVSSATFIT GDDDKDLASA
DDIEALIASF GAK
