(data stored in ACNUC1104 zone)

SWISSPROT: Q7WAA8_BORPA

ID   Q7WAA8_BORPA            Unreviewed;       685 AA.
AC   Q7WAA8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 114.
DE   SubName: Full=Chemotaxis protein CheA {ECO:0000313|EMBL:CAE36774.1};
GN   Name=cheA {ECO:0000313|EMBL:CAE36774.1};
GN   OrderedLocusNames=BPP1472 {ECO:0000313|EMBL:CAE36774.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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DR   EMBL; BX640427; CAE36774.1; -; Genomic_DNA.
DR   RefSeq; WP_010928053.1; NC_002928.3.
DR   EnsemblBacteria; CAE36774; CAE36774; BPP1472.
DR   KEGG; bpa:BPP1472; -.
DR   HOGENOM; HOG000255263; -.
DR   KO; K03407; -.
DR   OMA; KNTRGIA; -.
DR   BioCyc; BPAR257311:G1GSY-1512-MONOMER; -.
DR   Proteomes; UP000001421; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.10.287.560; -; 1.
DR   Gene3D; 1.20.120.160; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   Gene3D; 3.30.70.400; -; 1.
DR   InterPro; IPR004105; CheA-like_dim.
DR   InterPro; IPR037006; CheA-like_homodim_sf.
DR   InterPro; IPR036061; CheW-like_dom_sf.
DR   InterPro; IPR002545; CheW-lke_dom.
DR   InterPro; IPR015162; CheY-binding.
DR   InterPro; IPR035891; CheY-binding_CheA.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   Pfam; PF01584; CheW; 1.
DR   Pfam; PF09078; CheY-binding; 1.
DR   Pfam; PF02895; H-kinase_dim; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00260; CheW; 1.
DR   SMART; SM01231; H-kinase_dim; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00073; HPT; 1.
DR   SUPFAM; SSF47226; SSF47226; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF50341; SSF50341; 1.
DR   SUPFAM; SSF55052; SSF55052; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
DR   PRODOM; Q7WAA8.
DR   SWISS-2DPAGE; Q7WAA8.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669}.
FT   DOMAIN        3    108       HPt. {ECO:0000259|PROSITE:PS50894}.
FT   DOMAIN      330    538       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      540    675       CheW-like. {ECO:0000259|PROSITE:PS50851}.
FT   COILED       11     31       {ECO:0000256|SAM:Coils}.
FT   COILED      329    356       {ECO:0000256|SAM:Coils}.
FT   MOD_RES      50     50       Phosphohistidine. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00110}.
SQ   SEQUENCE   685 AA;  73597 MW;  B2DC71AB0B1FC420 CRC64;
     MSSGLDLSQF YETFFDEADE LLAQMEQLLL ELDVGAPDIE QLNAIFRAAH SIKGGAATFG
     CFQKLAGTTH LLENLLDAIR RGEMGLRADM VDIFLETKDV LKSQLDAYRA SEEPEDAVFE
     RICAVLRQLA LEGGQAPAAA APAPVAASEP GPEPEPAPQP AAASTAAGLP LRVRFSKVSD
     KDAQSLLEEM GNLGDVRASE RAGQTLTVWV DTTCSPDDIE AVCCFIIDAD QLEIAREAEP
     AHASAQAAVA AAPDAAATPA PVAAPAAAQA AEPARAARPS IAPAHADKES TSIRVGVEKV
     DQVINLVGEL VITQAMLAQT ASTLDPVLHD RLLNGMEQLE RNARDLQEAV MSIRMMPMDY
     VFSRFPRLVR DIAGKMGKQI ELQTYGRATE LDKSLIERII DPLTHLVRNS LDHGIETPDK
     RVAAGKEPVG QLVLSAQHNG GNIVIEVSDD GGGLSRERIL RKAVAQGLTV NENSPDDEIW
     QLIFAPGFST GDQVTDISGR GVGMDVVRRN IQDMGGHVQL SSVPGQGTTT RIVLPLTLAI
     LDGMSVRVGE ETFILPLNHV TESLQPQADQ IYSVAGNERV MQVRGEYLPL VEMHRVFSVG
     QAQADPTQAI AVIMQAEERR FALLVDHLVG QHQVVVKNLE SNYRKVPGIS AATILGDGSV
     ALIVDVFALA RANREKWSQP EAILN
//

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