ID A0A2N1DEW4_9ALTE Unreviewed; 721 AA.
AC A0A2N1DEW4;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CXF95_05660 {ECO:0000313|EMBL:PKH00117.1};
OS Paraglaciecola sp. MB-3u-78.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=2058332 {ECO:0000313|EMBL:PKH00117.1, ECO:0000313|Proteomes:UP000233828};
RN [1] {ECO:0000313|EMBL:PKH00117.1, ECO:0000313|Proteomes:UP000233828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB-3u-78 {ECO:0000313|EMBL:PKH00117.1,
RC ECO:0000313|Proteomes:UP000233828};
RA Collins E., Ducluzeau A.-L.;
RT "Pharmacopeia of the Arctic Ocean.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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:PKH00117.1}.
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DR EMBL; PJCF01000003; PKH00117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N1DEW4; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000233828; 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:UP000233828};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 1..104
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 322..573
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 575..710
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT REGION 144..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 721 AA; 79658 MW; 8223361F2FA15B28 CRC64;
MSIDMEQFHE VFFEESLEGL DVMEQALLII GQSNDPEVIN TIFRAAHSIK GGSGTFGFGD
VANFTHVLET LLDEARDGKR ELNEECIELL LRSCDCLRGM FTALQAKETP NLYQSIELIA
AFERILGATD KTVNTVQADA VTQTSQAGSG PMLSQNSKND ANTSSGTDNK VTKHWQIKFV
PEPQILLAGN EPLRLFRELA ALGDLATSAD ISEVPNFADL TVDECFIRWD LELSNSSASK
EDILEVFDWV IDECTLDIQL VGDNTSTQDN AMTSEPFEVP SVDIENMLTT NTEEPEQQFA
GADKKAAPEI RAPRSDKNTH PSSSSSIRVG IDKVDSLINL VGELVITQSM LSELGNNFDM
TKLERLFHGL EQLLQNTKEL QESVMRIRML PISFAFNRFP RMVRDVAIQI DKKVELVILG
ENTELDKTVM EKITDPLVHL VRNAIDHGIE TPEERIRKGK PEQGCIRLDA HHQGGNVVIE
VSDDGKGLNT LIIRNKAIEK GLIDSNEQLS DNEIYDLLFQ PGFSTAAQVS DISGRGVGMD
VVKRNIKSLG GRIVVQSKVD VGTTIKVHLP LTLAILDGQL VRVGQQVFII PLITIVESLQ
VKPELVNRVS GDMVMYRLRE DNVPIIYLYK EFDISADNTD IDNALLVVVE SDGQKIGLLV
DDLLAQQQVV IKSLESNYKR IEGISGATIL GDGSVSMILD IPGLITASCR RSNVKRQFKV
A
//
