ID A0A1V3NZL7_9GAMM Unreviewed; 1992 AA.
AC A0A1V3NZL7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chemotaxis protein CheA {ECO:0000256|ARBA:ARBA00021495};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B0E52_14205 {ECO:0000313|EMBL:OOG38393.1};
OS Rhodanobacter sp. C06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1945854 {ECO:0000313|EMBL:OOG38393.1, ECO:0000313|Proteomes:UP000189228};
RN [1] {ECO:0000313|EMBL:OOG38393.1, ECO:0000313|Proteomes:UP000189228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C06 {ECO:0000313|EMBL:OOG38393.1,
RC ECO:0000313|Proteomes:UP000189228};
RA Lycus P., Bothun K.L., Bergaust L., Shapleigh J.P., Bakken L.R.,
RA Frostegard A.;
RT "Phenotypic and genotypic richness of denitrifiers revealed by a novel
RT isolation strategy.";
RL Submitted (FEB-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:OOG38393.1}.
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DR EMBL; MUNP01000066; OOG38393.1; -; Genomic_DNA.
DR STRING; 1945854.B0E52_14205; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000189228; 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; 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; 4.
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; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF8; HISTIDINE KINASE; 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; 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; 2.
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; 5.
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; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OOG38393.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000189228};
KW Transferase {ECO:0000313|EMBL:OOG38393.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 673..780
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 863..974
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1206..1309
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1463..1696
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1698..1835
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1861..1977
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1005..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1475..1502
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1067..1095
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 720
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 907
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1253
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1910
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1992 AA; 216287 MW; 4222667FB59D0EC8 CRC64;
MRLQDHIDFT TLQWVRPELE QTLADAREAL ESYVDNPASD EAMRACASGL HQVQGTLRMV
ELPGPAMVAS EMEALAVALL EGHVAQREEA YTALMRGMMQ LPDYLERLAG GHRDVPVVLL
PLLNDLRASR GQEALPESAL FRPNLDAFLP TQAPAAMSEA QAEARRGELV ELRLQFQQHM
LAWFRGQSQA QPLAGMRKAL LAIAARCFHV HGRRLWWIAA GVVEGLERGM LVAHAAELRQ
LIGKADRHIR QLIEQGEDSL RGGEADDLCN RLLYIVAQSR QHSPHMELLR RTYALDNLLP
DADELEHARG SMAGHNRALL DSVAKALKDD LLRVKEALDL FQRQPGADAA SLEPQCELLG
RVGDTLGMLA LSVPRRVIEE QRRVLDEIVN KLRPVDEDIL LDVAGALLYV EASLDDHIES
LGAGEEPHDG TVAPGLPRSE AQGILSTVMQ EAVRNTEKVK EAIVAFVESG WEHAGLTAAP
AQMSEVAGAA RMLSAERPAE LAEGIGRFIH NELLADRRVP SSTQMDHLAD ALAALEYYLE
AAREHRGGLA HIIDVAEHSL GQLGYWPLPA ERPLSAVPVD APAAEVQDSG EDTLSESVSL
YPGSDASQLF VAPEVPREAP AHDVDGLRYA QTEATAPPMA GDDADWIEIE EEIEEQVPAN
AAQAGAFRFD HQAEGIDDDI REIFVEEMQE EIDNLRSAEG SWLADPARLD ALTPIRRSFH
TLKGSGRLVG IPALGEFAWR VEDMLNRVLD HTVEPHAGVQ ALVRHAIDAL PQLLASLKGE
GVPHAPVEAI QQTASRLAGG DASARIEDHA PTAMETVRRT VRRRVPRLDA AAAAIPAAGL
TDTQSVPAPE PAEPPVSLAI SPLPSVDPVL LEILRSEVAQ YLQAIRTAIQ RSSGELPVGE
DLLRAVHTLH GAIAMVEIPL LTQLLSPLES LLKRVRGVGQ ALPVEGVRLL DRSADVVDHV
MAQFDVATPQ LPNVDLLTTQ LIELRDRYPE SQVAHVGAEI HAEAAPSPVD FAAPADATDE
PEAPAVAEHT APASLPEDGA HDDYASELMA ALGAFEPQAP SLAEREAAEH AAAERLAAEH
AEAEQRAHAA AEQEAAERAA AEQAAQAKAE QEQAEREQAE QERLEQERIE QERAEQVRLA
QERAAREAAE AQMRAAAEKA AAEQRAAEAA AAEQARLDAQ REAEAARAAA VDHAAPVAAV
ALADTGLPID ADLLEVFVEE AREILDHADG VLAQWHAEPA AAGHLPELQR DLHTLKGGAR
IAGLMPVGDL AHAIETLLEK PVADAAQAIP LIGVLEASFD QLHTMVQQVS QGQAPTYPQS
TIDHLLALAG EQQFADDAAL AARAAPPAQP VVPLPELLPA AEGVDVPSAQ EQIRVRAELL
DNLVNHAGEV AIYRSRLEQQ VSGYRFNLVE LDQTVQRLRS QLRMLEIETE AQIIARFQRE
HREAGSATVF DPLELDRFSQ LQQYSRALAE SVSDLVSIQG MLDELTRQAE NLLVQQSRVS
TELQEGLLRT RMLPFDTMVP NLRRTLRQAA QEEGKSAQLY VDGAHGEMDR NLLDRIKAPF
EHMLRNAVAH GIESPAQRRK AGKPAEGAVR IRVAREATEV VVRVSDDGRG LDREAVRKRG
VERGLIRADA RLSDDQLLAL ITQPGFSTAS TVTQLAGRGV GMDVVANEIK QLGGSLAIES
QPGQGTTFVL RLPFTLAVTQ AILVRIGEST FAIPMTSVQG VARIGPDELA AKLAEHEPAF
GYNGEQYGIH DLAELLGLPP GAVPEGEQPP LLLTRAGDLR AAIRIDAVLG SREIVVKSVG
PQVSSVPGVL GATIMGDGSV LVILDLAPLV RHGVVRREQR LAEGLSAVEL PTIEELRARP
LVMVVDDSIT MRKVTGRVLE RHEYEVGTAK DGVDALEKLH ERVPDLMLLD IEMPRMDGYE
LATHMKADPR LRDIPIIMIT SRTGEKHRQR AFDIGVDRYL GKPYQEAELL TQIGEVLEQR
AMALLAREPH HA
//
