ID K9H296_9PROT Unreviewed; 992 AA.
AC K9H296;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C882_3422 {ECO:0000313|EMBL:EKV31672.1};
OS Caenispirillum salinarum AK4.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=1238182 {ECO:0000313|EMBL:EKV31672.1, ECO:0000313|Proteomes:UP000009881};
RN [1] {ECO:0000313|EMBL:EKV31672.1, ECO:0000313|Proteomes:UP000009881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK4 {ECO:0000313|EMBL:EKV31672.1,
RC ECO:0000313|Proteomes:UP000009881};
RX PubMed=23409257;
RA Khatri I., Singh A., Korpole S., Pinnaka A.K., Subramanian S.;
RT "Draft Genome Sequence of an Alphaproteobacterium, Caenispirillum salinarum
RT AK4(T), Isolated from a Solar Saltern.";
RL Genome Announc. 1:E00199-12(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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKV31672.1}.
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DR EMBL; ANHY01000005; EKV31672.1; -; Genomic_DNA.
DR RefSeq; WP_009539541.1; NZ_ANHY01000005.1.
DR AlphaFoldDB; K9H296; -.
DR STRING; 1238182.C882_3422; -.
DR PATRIC; fig|1238182.3.peg.1092; -.
DR eggNOG; COG0643; Bacteria.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000009881; Unassembled WGS sequence.
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; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.40.50.180; CheA-289, Domain 4; 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; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 3.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 2.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 3.
DR SUPFAM; SSF52172; CheY-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; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:EKV31672.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000009881};
KW Transferase {ECO:0000313|EMBL:EKV31672.1}.
FT DOMAIN 1..101
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 271..521
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 523..703
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 725..853
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 872..989
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 127..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 922
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 992 AA; 105979 MW; 82AAC214A0578042 CRC64;
MDDLLSEFLT ETSESLSTLD VELVNLEQNP NDRDILSNIF RLVHTIKGTC GFLGLPRLES
LAHAAENVLG KFRDGELEVT PAAVTLILTS IDRIKEILAH LEQTEQEPEG TDEDLKTQLN
AAAEGRLEEH QAGEDVGASA EPEGGAGDDA AADAGGDEAG GGPVLSDAGF PVAAELLAEV
EAATASGKKA ASEDELAAEM AAEMEKEAAA KEGAAAAPPP KEEAKKEQKS EAKPPAPAAK
PPAKAAQPPA KQGAGGGGGA GPEKKGSEPS IASQSIRVSV ELLENLMTLV SELVLTRNQL
LQMVRGRDDS EFTAPLQRLS HITSDLQEGV MKTRMQPIGN AWAKLPRIVR DLSIEMGKKI
DLQMYGAETE LDRQVLELIK DPLTHMVRNS ADHGLEDTEG RIAAGKPETG VVKLNAYHEG
GHIIIEISDD GRGLNIDKIR DKAIMNGLAT EAEMDNLTDQ QVAQFIFKAG LSTAEKVTSV
SGRGVGMDVV RTNIERIGGT VELKTWPGKG STFTIKIPLT LAIVSALIVE CAHERFAIPQ
ISVLELVRVT KNSETGIEMI SDAPVLRLRD RLLPLVSLGN LLKLRKKTVH EEVEDLIDAH
DGVPAGQAKG KGKGKGNGSA LDKVGAATNA DGDIAETFIV VTQVGTYTFG IIVDRVFDTE
EIVVKPVAPI LRHISMFSGN TILGDGSVIM ILDPNGIATA TGEVTMGTGT AAESTAQHDA
RGDDRTSLLV FRAGGKDLKA VPLALVARLE EVDCATVEHS YGKPVVQYRG QLMPLVTVNQ
GYEIPDEGRQ PVLVFSDRDR SMGLVVDEIV DIVEDRLKVE LKADKPGVIG TAIIGEKATD
VIDTGYYLTQ AFGDWFGNPD ESAPSLASGK KRVLLVDDSP FFRNLLTPLL SVAGYDVTSV
DGPQRALEMR EQGHDFDAII SDIEMPGMDG FGFAEAVRAD GRWADLPMVA LSSHATQKDF
ERGRQVGFDD YVTKFDRDAL LETLKATLGS RS
//
