ID A0A0F4QDF2_9GAMM Unreviewed; 707 AA.
AC A0A0F4QDF2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=TW77_21805 {ECO:0000313|EMBL:KJZ05743.1};
OS Pseudoalteromonas rubra.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=43658 {ECO:0000313|EMBL:KJZ05743.1, ECO:0000313|Proteomes:UP000033452};
RN [1] {ECO:0000313|EMBL:KJZ05743.1, ECO:0000313|Proteomes:UP000033452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2471 {ECO:0000313|EMBL:KJZ05743.1,
RC ECO:0000313|Proteomes:UP000033452};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(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 -!- 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:KJZ05743.1}.
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DR EMBL; JXYA01000063; KJZ05743.1; -; Genomic_DNA.
DR RefSeq; WP_046007071.1; NZ_JXYA01000063.1.
DR AlphaFoldDB; A0A0F4QDF2; -.
DR PATRIC; fig|43658.5.peg.4593; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000033452; 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:UP000033452};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 308..550
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 552..687
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 128..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 707 AA; 78348 MW; D32F80C6138E7EF7 CRC64;
MSIDLSQFFD VFFEESFEGL DAMESELLNL EPGKEDQETI NTIFRAAHSI KGGSGTFGFT
AVSDFTHVLE TLLDQIRNGQ RQLTAEHVNL LLKAVDCLRA MLTALQAQQE PEQQEANELK
QRFEAILNGD SRTDEQGQAT STSDDTSEEQ AHLPITFQID FKPLPYLFKT GNEPLYMIAE
LSELGELETQ ALHDELPKFK QLTPDDCYLY WRFFLTTTRG EAAIREIFEW VEDDAEITIV
QCGGLFDAPA EPTAQVDMLP DEQAEPELPL EINVPQKPLH EVKKEPSAGK DARKNADPST
TSIRVGIDKV DSLINMVGEL VITQAMLSQI GEQEITESSI AALQEGLAQL AHNTRDLQEN
VMRIRMLPIS FVFSRFPRLV RDISQKLNKQ VELKLIGEQT ELDKTVMEKL SDPMVHLVRN
SLDHGLETPE QRIAQGKDPV GTVTLNAFHQ GGNIVIEIMD DGKGLDTDKI RKKAIQNGLI
QAQDELSVDE INELIFMPGF STADNVSEIS GRGVGMDVVR KNIQALNGSV EVSSEAGVGS
TFTIRLPLTL AILDGQLVQV AEHTYIIPLI SIVESLQIDI TKVSNVGKGL QVLRLRDEYI
PILRLYDIFN HKGAREELDK TLLVVVENDN YKVGILVDDL LAQQQVVIKS LEANYQRVDG
ISGATILGDG TVSLIIDISG LIKLSGLRRP GSSELLVDLK TDEGIPA
//
