ID   CHPEP_HELPY             Reviewed;         505 AA.
AC   O25089;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Chemotaxis regulatory protein ChePep {ECO:0000303|PubMed:21791582};
GN   Name=chePep {ECO:0000303|PubMed:21791582}; OrderedLocusNames=HP_0322;
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, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=21791582; DOI=10.1128/mbio.00098-11;
RA   Howitt M.R., Lee J.Y., Lertsethtakarn P., Vogelmann R., Joubert L.M.,
RA   Ottemann K.M., Amieva M.R.;
RT   "ChePep controls Helicobacter pylori Infection of the gastric glands and
RT   chemotaxis in the Epsilonproteobacteria.";
RL   MBio 2:0-0(2011).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CHEZ.
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 essential role in chemotaxis. Regulates flagellar
CC       rotation through the formation of a complex with chemotaxis protein
CC       CheZ (PubMed:21791582, PubMed:26061894). Plays a major role in
CC       colonization of the stomach (PubMed:21791582).
CC       {ECO:0000269|PubMed:21791582, ECO:0000269|PubMed:26061894}.
CC   -!- SUBUNIT: Interacts with CheZ; the interaction is essential for each
CC       other polar localization. {ECO:0000269|PubMed:26061894}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21791582,
CC       ECO:0000269|PubMed:26061894}. Note=Localizes to the cell poles.
CC       {ECO:0000269|PubMed:26061894}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutants cannot control the rotation of
CC       their flagella and swim with abnormally frequent reversals.
CC       {ECO:0000269|PubMed:21791582}.
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DR   EMBL; AE000511; AAD07390.1; -; Genomic_DNA.
DR   PIR; B64560; B64560.
DR   RefSeq; NP_207120.1; NC_000915.1.
DR   RefSeq; WP_000782061.1; NC_018939.1.
DR   AlphaFoldDB; O25089; -.
DR   SMR; O25089; -.
DR   IntAct; O25089; 1.
DR   STRING; 85962.C694_01630; -.
DR   PaxDb; O25089; -.
DR   EnsemblBacteria; AAD07390; AAD07390; HP_0322.
DR   KEGG; hpy:HP_0322; -.
DR   PATRIC; fig|85962.47.peg.344; -.
DR   OMA; CMYKKGH; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome.
FT   CHAIN           1..505
FT                   /note="Chemotaxis regulatory protein ChePep"
FT                   /id="PRO_0000448753"
FT   REGION          154..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..349
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..402
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..463
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   505 AA;  58469 MW;  B7633BA416820C70 CRC64;
     MKMILFNQNP MITKLLESVS KKLELPIENF NHYQELSARL KENQEWLLIA DDECLEKLDQ
     VDWLELKETI SQNKNSVCMY KKGNEAQPFL EGFEVKIKKP FLPTEMLKVL QKKLGSNASE
     LEPSQNLDPT QEVLETNWDE LENLGDLEAL VQEEPNNEEQ LLPTLNDQEE KEEVKEEEKE
     EVKEEEKEEV KEEEKEEVKE TPQEEKKPKD DETQEGETLK DKEVSKELEA PQELEIPKEE
     TQEQDPIKEE TQENKEEKQE KTQDSPSAQE LEAMQELVKE IQENSNGQEN KEKTQESAEI
     PQDKEIQEVV TEKTQAQELE VPKEKTQESA EALQETQAHE LEKQEIAETP QDVEIPQSQD
     KEVQELEIPK EETQENTETP QDVETPQEKE TQEDHYESIE DIPEPVMAKA MGEELPFLNE
     AVAKIPNNEN DTETPKESVT ETSKNENNTE TPQEKEESDK TSSPLELRLN LQDLLKSLNQ
     ESLKSLLENK TLSIKITLED KKPNA