ID A0A2U2MYW3_9GAMM Unreviewed; 2128 AA.
AC A0A2U2MYW3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DEM34_14120 {ECO:0000313|EMBL:PWG61992.1};
OS Spiribacter halobius.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Spiribacter.
OX NCBI_TaxID=2182432 {ECO:0000313|EMBL:PWG61992.1, ECO:0000313|Proteomes:UP000245474};
RN [1] {ECO:0000313|EMBL:PWG61992.1, ECO:0000313|Proteomes:UP000245474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E85 {ECO:0000313|EMBL:PWG61992.1,
RC ECO:0000313|Proteomes:UP000245474};
RA Zheng W.-S., Lu D.-C., Du Z.-J.;
RT "Spiribacter halobius sp. nov., a moderately halophilic bacterium isolated
RT from marine solar saltern.";
RL Submitted (MAY-2018) 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:PWG61992.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QFFI01000024; PWG61992.1; -; Genomic_DNA.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000245474; 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; cd00088; HPT; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 5.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
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; 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; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 4.
DR Pfam; PF00072; Response_reg; 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; 4.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 6.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 4.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000245474};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 638..742
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 957..1060
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1184..1288
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1343..1450
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1608..1841
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1843..1982
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2005..2121
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 575..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1471..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1613..1647
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 907..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 685
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1003
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1231
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1390
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2054
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2128 AA; 224194 MW; 7EBF3F0C493EF06C CRC64;
MSMSSEIDHS TLRWVKKELD ETLREAAAAL ERFSEDPADA TQAQFCIAQL HQVRGILQML
ELHGAAMLTE EMEQLGAALL EGDAARGESG AEVLMGAILR LRDYLERLEG GQQDAALLIL
PLVNELRAAR GEAIIAESAL FSPDLGRAPE MPRHDRDGAD HLPEVAGAAR TLFQRGLLGF
LRGQGVRQGL ERMREAADQL DAAAPDDRTG AVWWVVGTVA EALAAGALNA DAAVRNLIGQ
VDRQIKAVAR HGAEAERPEA LMRGLLYYLA GAAPATPRIE AVQTHYDLPA LIADQQRLEQ
AREGLFGPGV DAFRSVAEAI REDLAGVKDT LDLYVRGSAR EPERLGAAAD AMRRIADTLG
VLGLAAPRRV VLEQAELVRG LEGSDDDALT VMKAAESLLY VESALQGLGG RAREGADGGP
AAAPETPEAA LFRSEYREVV ALTLDEAITE VGRVKEAIVR FLESHDGVQL EGLDERFASI
RGALGIMELP RAAALVGAAA HYVTERLASD ETPPPAEALD DLADAVTSIE YYLEALRDGR
SGAAQVLDVA ENGLRRLGEA LPAAAVSAGA TAEPAPTAAE SAADDAAVAE SEASAGPAET
VTDEAAPPAP DRPATQPDAA IDFSRKRGRV DLDVPVRADE LDAEIVEIFV EEAGEVLETL
AESFPRWRAN PDDEPALLTT RRMFHTLKGS GRLAGALLLG ELAWAVENLL NRILDRSREA
DESVFDVVKR SIDAVPGLLQ EFQGGAAPAT DVRGLMREAA RLADPASAVE AEGGDEEADT
AAAAAAADEP DADTSAGDEG PASEAMEPGS DAAGAADADA TETGSEDAAS EAAGFDAGEG
TAAPATADAG EDEVGAPVPG ADEPLPAGDP AGHGEATEQT AAPERADAAD AESAAGADGP
TVVDEDTGDD AAGHETADHV EAAGEHETAD GAEAVAEPEG NREPEAAGDA ESETAALPAM
DPILYDIFSK EAEDHLAAVD AFLARAAAGD SLRVSHDVIR SLHTLTGSAR MADVEPIARL
GRRLEDLARI RFADRRPLSG DELEVIERSV ARVREIVAAL GRAGFPVPDV DGLVAEVDAL
KGGAPVPSLE AVTDDTEVPP DAGEPAFEAE GPEERADGAA SADEGRETDA EFSRDDSSEY
RAELDAPGAD SAHADGDEAA ETLGFEAPPA EDPADDAAGM ALAAAEDDAE LRAIFLEEAE
ELRGHIESLL ADWEAGDGGD APAESLQRAL HTLKGGARLA EQAGIARLCH AMETLAAAVA
EEGLAADGTF FRLGQRATDH LGDLLRQAAD DVVPEADEAL VAALEDAADA PADTGDTGEA
LAASDTEPES ASPVTGTTDA EAEPPPDEEL VEVFLEEAGE ILAALEAHLN EWREGADEES
TLVALQRALH TLKGGARMAG FQPVANLAHA LETLLREVQE GGVAADPALF ELLEAANDAL
VAQREAAEAG RPVAAESALV ARIEAMTAGA APAAGPAPAP DPEAPEADTA GQAEVAAAPA
AEPPAADESQ RRQGDVVRVR SELLDDLVNF AGEVSIYRAR LEQQAGAIGF NLGELGQTVR
RLRDQLRTLE IETEAQILHR AEREYELQDR YGEDFDPLEM DRFSQIQELS RALSESVNDL
SSIEGTLDNL NRESETLLLQ QSRVNAELQD GLMRTRMVPF ANLAPRLRRI VRQASQELGR
EARLRVLGAE GEMDRTVLER IVPPLEHMLR NAVAHGIEAP EVRRAAGKPE GGTISVSLAR
EGADVVIRVA DDGGGMDLAA IRRKAVRQGL MNEDSTLTDR EVMQFVLESG FSTAEEVTQI
AGRGVGMDVV NAEIKQLGGN LEIDSTPGEG TRFTVRLPFT LALNQALLCE AGDEVYAVPL
SSVEGVVRMT GDEVNRRLDD PDGGRYEYAG TSYALRSLSG VLGAEEAPRP APGSRVPLLL
VQAGESRMAL QVDGLLGSRD IVVKSPGPQI ASVPGVLGAT ILADGRVVLI LDVSALVRFG
MLGDAPARPR IPAARAGGRG DRRSLVMVVD DSITMRKVAS RLLERNDIDV ITAKDGVDAV
AALQDRVPDA MLLDIEMPRM DGYEVAVHMR NDPRLRDVPI VMITSRTGEK HRQRALDIGV
DRYIGKPYQE GDLLATVREL LEHGRASA
//
