ID A0A061SX33_9RHOB Unreviewed; 736 AA.
AC A0A061SX33;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PM02_00115 {ECO:0000313|EMBL:KAJ04668.1};
OS Sulfitobacter mediterraneus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=83219 {ECO:0000313|EMBL:KAJ04668.1, ECO:0000313|Proteomes:UP000027337};
RN [1] {ECO:0000313|EMBL:KAJ04668.1, ECO:0000313|Proteomes:UP000027337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1FIGIMAR09 {ECO:0000313|EMBL:KAJ04668.1,
RC ECO:0000313|Proteomes:UP000027337};
RX PubMed=24855294;
RA Mas-Llado M., Pina-Villalonga J.M., Brunet-Galmes I., Nogales B., Bosch R.;
RT "Draft Genome Sequences of Two Isolates of the Roseobacter Group,
RT Sulfitobacter sp. Strains 3SOLIMAR09 and 1FIGIMAR09, from Harbors of
RT Mallorca Island (Mediterranean Sea).";
RL Genome Announc. 2:e00350-14(2014).
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:KAJ04668.1}.
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DR EMBL; JEMU01000001; KAJ04668.1; -; Genomic_DNA.
DR RefSeq; WP_051583963.1; NZ_JEMU01000001.1.
DR AlphaFoldDB; A0A061SX33; -.
DR STRING; 83219.PM02_00115; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR Proteomes; UP000027337; 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00110};
KW Reference proteome {ECO:0000313|Proteomes:UP000027337}.
FT DOMAIN 4..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 306..583
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 585..721
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT MOD_RES 51
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 736 AA; 78947 MW; 082840F8B9F735FE CRC64;
MTVDNDPMAE IRASFFIESE ELLEALQDGL QLMDDGAADN ETINVVFRAV HSIKGGAGAF
GLEGLVHFAH RYETVLDEVR AGRLQVETEA LKVFFQAADH LSDLVRISRD NDPLPDEETE
VLLKALDAFL GDTGPVSGTA EEDIEFQPMG LSLDLDLPVG DTADLPDLDA LPPLDLGPVT
TTYEITFAPQ ADLFDTGNEP ATLLRNLQQL GTAKVTCDSS RLPPLDQLRP DVPHLSWTVI
LQTDVEESEI VSIFEFVEGL CQLDIKKQGE PDGSDLPPLP DLPPVEPTIV EHPETLPQTP
IEVTPAPPAP VDDPVSTIAA PTQPAQATAP TAAKSVVRVD LDRIERLVNL VGELVINQAM
LSQSLEHSGL SPHSDAMSGL EEFQRLTRDI QDSVMMIRAQ PVKSLFQRMS RIVREASAAV
EKDVRLVTTG EATEVDKTVI ERLADPLTHM IRNAVDHGLE TKEERLAAGK PAQGKVNLSA
AHRSGRVVIE IADDGAGIDR PKVLQLAIDK GLIPPDSNLT DTEIDNLLFL PGFSTAATVS
NLSGRGVGMD VVRTSIQALG GRITTTSLPG QGTTFSISLP LTLAVLDGMV IEVAEETLVL
PLNLVIETLT LQRGDVEMVR PGRNVVRVRS GFVPLFDLGA ALGYRPPLDD FEGSVVLLIA
NEDETNAALL IDNILDQRQV VIKGLDESFY RAPGIAAATI LGDGQIALIL DPSDIISTAI
PKPGLSQTSS DAGVPA
//
