ID K0CH12_ALCDB Unreviewed; 667 AA.
AC K0CH12;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:AFT71665.1};
GN OrderedLocusNames=B5T_03398 {ECO:0000313|EMBL:AFT71665.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71665.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT71665.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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}.
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DR EMBL; CP003466; AFT71665.1; -; Genomic_DNA.
DR RefSeq; WP_014995727.1; NC_018691.1.
DR AlphaFoldDB; K0CH12; -.
DR STRING; 930169.B5T_03398; -.
DR KEGG; adi:B5T_03398; -.
DR PATRIC; fig|930169.3.peg.3358; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_3_6_6; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000006286; 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; 3.30.70.400; CheY-binding domain of CheA; 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; 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 PANTHER; PTHR43395:SF10; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
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; 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 Kinase {ECO:0000313|EMBL:AFT71665.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000006286};
KW Transferase {ECO:0000313|EMBL:AFT71665.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..103
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 258..508
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 510..645
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 135..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 667 AA; 71810 MW; B99A1D6DE1DCAE90 CRC64;
MDISDFYSTF FEEAEELLGD MEAHLLALDV DNPDMEQLNA IFRAAHSIKG GAGTFGFEAL
QRTTHLLENL LDYTRRGELT LRRDIVDTFL EAKDMLHDQL DAYRQGVEPD AEAMARICEV
LQKLALEEIG EPAGDVAPAT TVAPSTPPPA SGGTGQSLSV ALLGVSESDR KLLIEELGQL
GDVLETRGED DRYEVLMKST ASADDIEAVM CFIVEPEQLD IRSIPPEQLP VPVKTPEPQP
KAETKSAARP AVDSRDGGAN SSIRVPVAKV DHIINLVGEL IITQSMLNQV VEDSEFTGDA
GFASGLSLLQ RTARDLQEAV MSVRMVPMDY VFSRFPRLVR DLAGKLGKDV ELITEGKSTE
LDKSLTERII DPLTHLVRNS LDHGLETPEL RAAAGKPGTG RLTLSAQHQG GNILIEVSDD
GAGLDRERIL AKARSNGLPV SDNMSDEEVW QLIFAPGFST AEAVSDVSGR GVGMDVVKRN
IQAMGGHVDV ISEAGQGTRT RIVLPLTLAI LDGMSVRVGE ETFILPVSAV IESLQPRADD
LYTMAGGDVL LKVREDYLPL VALHHAMEVS GAVTDPTSAI VVIVQGEGRR YALLVDELVG
QQQVVVKNLE TNYRKVPGVS AATILGDGSV ALILDIPDLH RLSQSKKASD AVARNSTVLS
SKEVSAS
//
