ID A0A328VGZ2_9CHLR Unreviewed; 876 AA.
AC A0A328VGZ2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-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=A4R35_16840 {ECO:0000313|EMBL:RAQ97208.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ97208.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ97208.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ97208.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-2016) 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:RAQ97208.1}.
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DR EMBL; MCIF01000002; RAQ97208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328VGZ2; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000248706; Unassembled WGS sequence.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00088; HPT; 1.
DR CDD; cd00156; REC; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR036641; HPT_dom_sf.
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; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00260; CheW; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR PROSITE; PS50894; HPT; 1.
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:UP000248706}.
FT DOMAIN 81..189
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 753..869
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 284..311
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 129
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 802
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 876 AA; 95698 MW; E4E149540E8C5BC7 CRC64;
MAEPEDALQG DLPEPELPEG ASGLTPEDLA IIEAFRLMED LEPPVSLAEA AVTAGGDVGL
SDEAAATSTG GEEARAGLSS ADTGLDDMLA LFVAEADEDI ASMRQALTQL EQEDRLDEGH
LEALRRCAHK LKGTAGAVGC PSMSTIAYYI EMLVGSLRDG SVPMMIGLMA LVQAMRALEA
TLQSIVETGQ ESSAPLTELE ADYEALNEFG SVRRTPSESL MALTAADEAL LLEEEELAPR
SPLREEIARF HLRTRTPRES GSPLPSVLVD AERLKRLILH SEHLAEQREP LENARRELEA
ALQELYSAQA RLQYLETLLS LNPLSLSETG QVPPLPLRAL PQQPMSSLVR RILEEAEQAG
RHLPTHAQQR QRLSALALKA RETTSWDEME VDRYTESDVL LRAFAEAIAD VSTASAQVRA
AFTRLDRVLR RHMDLANRVR GETLLLRSAP LAVLLPRIRR AIRMSADAQR QRVRFEARGE
TTEVDQDILE ALARPLLQLV RYGMITNWGS VQAEDGAEEE QERRVWFYAH AVGNEVSLEL
GFSTPVRAGA LELVQGPIQQ LQGTVTAQRN ALGGVTFYLT LPRLHGAMHG LLVRTAGQRL
VVPFSQVRRI VVERSALEEE GQVSPACFPK DGRSAVPLSR LLGLPDVNGG GSPPVSAEEA
RPLLLLQEGL PYEVVEVDEV LGGVELVVRP VASYLRRPGI MGAAIDGQGN VLLVLDLMRL
VPPPEALDAE KAKAQREPLV GSPEQMATGV GRTVMIADDS VYIRQSLQQT LQRAGYRVVQ
ARDGMEAWEL LLEQPPDVLL LDIEMPHLNG YELLSMIRAS SRFASLKIIM LTARSSEKHR
RSAQDLGAQA YLIKPSPPEL LLDTIGAVLS EKPPAP
//
