ID A0A0D3VD43_9BACL Unreviewed; 662 AA.
AC A0A0D3VD43;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=UB51_14785 {ECO:0000313|EMBL:AJS59521.1};
OS Paenibacillus sp. IHBB 10380.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1566358 {ECO:0000313|EMBL:AJS59521.1, ECO:0000313|Proteomes:UP000032320};
RN [1] {ECO:0000313|EMBL:AJS59521.1, ECO:0000313|Proteomes:UP000032320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 10380 {ECO:0000313|EMBL:AJS59521.1,
RC ECO:0000313|Proteomes:UP000032320};
RX PubMed=25908145;
RA Pal M., Swarnkar M.K., Thakur R., Kiran S., Chhibber S., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequence of Paenibacillus sp. Strain IHBB 10380 Using
RT PacBio Single-Molecule Real-Time Sequencing Technology.";
RL Genome Announc. 3:0-0(2015).
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};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP010976; AJS59521.1; -; Genomic_DNA.
DR RefSeq; WP_044877953.1; NZ_CP010976.1.
DR AlphaFoldDB; A0A0D3VD43; -.
DR STRING; 1566358.UB51_14785; -.
DR KEGG; pih:UB51_14785; -.
DR PATRIC; fig|1566358.3.peg.3285; -.
DR HOGENOM; CLU_000650_3_6_9; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000032320; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
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; 3.30.70.1110; Histidine kinase CheA-like, P2 response regulator-binding 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; IPR037052; CheA-like_P2_sf.
DR InterPro; IPR010808; CheA_P2-bd.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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 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 Pfam; PF07194; P2; 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; SSF55052; CheY-binding domain of CheA; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000032320};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..102
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 323..528
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 530..662
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 45
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 662 AA; 74434 MW; AE3C5B83F668B94F CRC64;
MLSEYKEVFL EELEEQLQLM DDVILQLEQK GETERVVQSL FRAAHTLKGS SAAMGYEEMK
QLTHEMEHLL DLVRSKVLRV TDTLIDLLFQ SLDCLKELKK DIMRSDDSTT DISGCVRDLQ
AFAKSPKESI PQEMEDLLKP ELSLDTTLKI QEAEDQGLKV FWICVKISLE CVIKGARFYL
IQSHLCEWGD VLYSLPDIER IGEEGNETAE VQFLYAGNQS NQELQDLVGA LTEVTDVKIE
SLSTEMTVSV DKEIERQETI VNEHQTYKAK SKTQTIRVSV ERLDHLMNLV GELVIDHTRI
DQVERMQRRQ FSDDSLEELS QISDHLSSII GDLQESVMKA RMLPIEQLFN RFPRMIRDLT
RDLGKDIELV IGGKDTELDR TLIEEIADPL IHLIRNAVDH GIELPEQREQ SGKQRKGTLQ
IKAAHEDNQV VIYVTDDGAG IDPTKMRKSA LDKGIISSEE AVLLSDREAI HLIFRPGFST
ASRVSDVSGR GVGMDIVRSH IEKLNGLIDI DTELGQGTCF KIKLPLTLAI IIGLLVKLNG
QTFIIPMSNI AEIIRITNND IETVRGQSVV LLRNQIIPIV WLHDHFNIPR GKQRKGHIQL
VIVGSAEKRL ALAVDELIGN QEIVIKSLGP YIGKINGIAG STILGNGKVA LIIEVSGIIN
QR
//
