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Database: UniProt
Entry: A1WZ19_HALHL
LinkDB: A1WZ19_HALHL
Original site: A1WZ19_HALHL 
ID   A1WZ19_HALHL            Unreviewed;       703 AA.
AC   A1WZ19;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Hhal_2167 {ECO:0000313|EMBL:ABM62931.1};
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124 {ECO:0000313|EMBL:ABM62931.1, ECO:0000313|Proteomes:UP000000647};
RN   [1] {ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hoff W.,
RA   Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABM62931.1, ECO:0000313|Proteomes:UP000000647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1 {ECO:0000313|Proteomes:UP000000647};
RX   PubMed=23991253; DOI=10.4056/sigs.3677284;
RA   Challacombe J.F., Majid S., Deole R., Brettin T.S., Bruce D., Delano S.F.,
RA   Detter J.C., Gleasner C.D., Han C.S., Misra M., Reitenga K.G.,
RA   Mikhailova N., Woyke T., Pitluck S., Nolan M., Land M.L., Saunders E.,
RA   Tapia R., Lapidus A., Ivanova N., Hoff W.D.;
RT   "Complete genome sequence of Halorhodospira halophila SL1.";
RL   Stand. Genomic Sci. 8:206-214(2013).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. CheA is autophosphorylated; it
CC       can transfer its phosphate group to either CheB or CheY.
CC       {ECO:0000256|ARBA:ARBA00035100}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP000544; ABM62931.1; -; Genomic_DNA.
DR   RefSeq; WP_011814953.1; NC_008789.1.
DR   AlphaFoldDB; A1WZ19; -.
DR   STRING; 349124.Hhal_2167; -.
DR   KEGG; hha:Hhal_2167; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_000650_3_6_6; -.
DR   OMA; MMDMAKS; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000000647; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   CDD; cd00731; CheA_reg; 1.
DR   CDD; cd16916; HATPase_CheA-like; 1.
DR   CDD; cd00088; HPT; 1.
DR   Gene3D; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 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; 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   PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR   PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR   Pfam; PF01584; CheW; 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; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF50341; CheW-like; 1.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50851; CHEW; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABM62931.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000647};
KW   Transferase {ECO:0000313|EMBL:ABM62931.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          1..105
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          336..549
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          551..686
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          128..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          332..366
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         48
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   703 AA;  75635 MW;  CE7EC3EB302C7284 CRC64;
     MSVDLSQFLQ TFFEESFEGL DTMESGLLEL DPESPDPEAL NNVFRAAHSI KGGAGTFGLS
     AVSDFTHRME TLLDRLRDGK QAVTPDCVNV LLNAVDCLRG MLVAIQSDQT LDADAISTAQ
     QRLDEQLGQA PVGGGGATGA AAGPTAGGGD AGGDDAPPPR GGGGGGGWLI RFEPQPHLFA
     TGNDPRRLFL ALQDLGELEV ECDTSGLPPF EQLDPETCQL AWTLRLYADV PEAAVREVFE
     WVEDDARLEI QPLEAAGTEE VAPVAPGQPP MPTSEESGPA APAAGGGEAR KPAARRGGGN
     SSIRVDTEKI DALIDMVGEL VITQSMLSQV GKEFTAERLE ELQDGLAQLE RNTRELQENV
     MRIRMVPISF AYSRLPRIVH DTSRALGKAV DFQMEGEQTE LDKTVMEKII DPLVHLVRNS
     VDHGIEPPEE RAAAGKPETG TITIEAYHKG GNIIIEIADD GRGINRDKLL AKARSSGLLE
     DGTELPDDQV FDLIFHPGLS THEQATEYSG RGVGMDVVKR NVRSLSGNIH VRSAQGQGTT
     ITISLPLTLS ILDGQLFRVG DQTYIVPLVS VIESLQVDGS KLSRVTGRGE VYHWREGYVP
     IVRLHELFDT EPVRRELAGG LMVIVEDEDT YLGVFVDDLL DQQQVVIKSL EANYLQVPGI
     AGATILGDGT VALILDIAGL IEMSRGGRRQ PYIPTPEDSD EAA
//
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