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Database: UniProt
Entry: B3PIJ8_CELJU
LinkDB: B3PIJ8_CELJU
Original site: B3PIJ8_CELJU 
ID   B3PIJ8_CELJU            Unreviewed;       759 AA.
AC   B3PIJ8;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 95.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=cheA {ECO:0000313|EMBL:ACE84683.1};
GN   OrderedLocusNames=CJA_2138 {ECO:0000313|EMBL:ACE84683.1};
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84683.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE84683.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84683.1,
RC   ECO:0000313|Proteomes:UP000001036};
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE84683.1; -; Genomic_DNA.
DR   RefSeq; WP_012487740.1; NC_010995.1.
DR   AlphaFoldDB; B3PIJ8; -.
DR   STRING; 498211.CJA_2138; -.
DR   KEGG; cja:CJA_2138; -.
DR   eggNOG; COG0643; Bacteria.
DR   eggNOG; COG2198; Bacteria.
DR   HOGENOM; CLU_000650_3_7_6; -.
DR   OMA; NELVECC; -.
DR   OrthoDB; 9803176at2; -.
DR   Proteomes; UP000001036; 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:SF1; 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   Kinase {ECO:0000313|EMBL:ACE84683.1};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW   Transferase {ECO:0000313|EMBL:ACE84683.1};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          2..106
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   DOMAIN          406..615
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          617..751
FT                   /note="CheW-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50851"
FT   REGION          324..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         49
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   759 AA;  80857 MW;  2696E1C1BD515C7F CRC64;
     MSFGDDEDIL QDFLVEAGEI LERLNQQLVD LEQRPEDKDL LNAIFRGFHT VKGGAGFLSL
     TPMVECCHVT ENLFDILRNG KRTVTSELMD VVLQALDMVN QQFELVSQRE ALPPVDPTLI
     AALERLVSCA DLVEVAPASV VTPAPSPAQG KAAPVAEGDI TDEEFEQLLD AITGTPANPS
     TPAAAVTASS DEITEEEFES LLDQLHGKGK GPGVVVPAPA PVANTPASGN EITEDEFEAL
     LDQLHGKGKG PGTSPAVAAA PAVPVASSVS TVSAPAPETI GSDAINEDEF EALLDQLHGK
     GKGPSSEANA SAASVAAPAI NKPAPVKASS TVAPEVKPAK SEPDRDTGKK VEPAKPAAAA
     ADAPQVETTV RVDTQRLDDI MNMVGELVLV RNRLVRLGSS SNNEALAKAV ANLDVVTADL
     QTSVMKTRMQ PIKKVFGRFP RVVRDLARSL RKEINLELVG EETDLDKNLV EALADPLVHL
     VRNSVDHGIE FPDVREANGK PRTGQVVLAA EQEGDHILLS ISDDGAGMDP VRLRRIAVEK
     GMFDEDTANR LSDTEAYNLI FAPGFSTKKE ISDVSGRGVG MDVVKTKIAQ LNGTVEIKSE
     LGKGTRFVIK VPLTLAIMPT LMFMLGGQTF AFPLVSVNEI FHMDLTKSHV VDGQDCIAIR
     DQAIPLFYLK DWLVKGAYGE HPDNAHVVIV TVGTRRVGFV VDQLIGQEEV VIKPLGKMLQ
     GTPGMAGATI TGDGTIALIL DIPSLLRRYA RGSTSWGHS
//
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