ID A0A1H7SJE2_9GAMM Unreviewed; 2513 AA.
AC A0A1H7SJE2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05428989_2347 {ECO:0000313|EMBL:SEL72578.1};
OS Pseudoxanthomonas sp. GM95.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=1881043 {ECO:0000313|EMBL:SEL72578.1, ECO:0000313|Proteomes:UP000199164};
RN [1] {ECO:0000313|Proteomes:UP000199164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM95 {ECO:0000313|Proteomes:UP000199164};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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};
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DR EMBL; FOAX01000002; SEL72578.1; -; Genomic_DNA.
DR STRING; 1881043.SAMN05428989_2347; -.
DR Proteomes; UP000199164; 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; 2.
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; 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 PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:SEL72578.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SEL72578.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 823..930
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1452..1556
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 2003..2236
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2238..2371
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2390..2506
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1310..1329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1643..1672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1688..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1936..1970
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1654..1670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 870
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1499
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2439
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2513 AA; 266938 MW; 514E4634F4A021AE CRC64;
MSALREAMSH AVLGWVKPEL DQTLRLVRGE IESFADNPAD TSRMHVCVGY LHQVQGTLHM
VELYAPAMVA EELEKLAQAL QAGQVADADE ACATLMRGTV LLPDYLERLQ SGHRDIPIVL
LPLLNDIRAS RGETGLSESV LFAPDLNRPL PQDVPAIEPM PGNTRDTRFA QAHEHLERVL
AHWPEDGAPA DASALVAVLM PLQRLTQHTA VRRMLWVAVS VAEALRDGAL APTPALQQGF
TGVLRAVRQI KQGVVPGAAP GQEPTRQLLY QVAHSPAMHP ALDDLRKAFD LEAAASPSEA
ELEHARSSIS GRNRALLDTV GGAVKEELMR VKDALDLQLR TGADIAGLAP QVTQLASVAD
TLGMMGLGLA RNVVLQQRDS LAELVDGRRA AEEGALMDIA GALLYVDASL DDQVTHLGEN
TAPDTQTVEA QRTVEALAGE AIRNFSEARQ QFVAFIETGW DHDQLQDMPR LLGEVGGALR
MLELEEPADY LEGVRRYIGT ELIQRQRVPG GAQLDTLADA MASLEYYLEA LREHRPNREE
ILGITRSSLE TLRYWPLPSE QDAPAPMALA PQDDAPAVQR DATPLTFAPA PEFTADALDS
SPIDSADEAP AFSIERAPEL PEFVPAQASD NGFDPVAGEF DALAPTAAEE ADQIDAAFAS
DEAALVEAAF EPVSPVASEV ESGADVPVAF DAGDDAPVAH EAEPEVAPVF ELPVDGLVSP
EPPELPAFTE PTPEPVAEVA PSFDAAFEPE TIEPESVAAD ALEAPIDSFD VEAIEMIEAT
DVVTPAEAIE PINAGNAVEA IDATDVALAD NGQLLEGGFD LTGNDIDDEI RDVFLEEFDE
EIGNLREMLP AWTSHVENLD RLRPIRRVFH TLKGSGRLVG ARLLGEFAWK IENMLNRVLD
GSRPASPAVV ALLEQATDTL PQLNAALRGH TGVQADLAGI EAMADRVAAG EDVFYRPQAT
AQAPAAVEAP TEATAAPVFV PDLDGTPASV DSVLREILET EVNNHLQTVD AWLEPALAAG
TAVATDPLLR AFHTMNGAFA MADVPEITEI TGRAEQYVKR LLANGVAADA AGVAGLSGAA
AAIRTAIAAL QESQPRIPLF SDLRAELGAL RDSLPQVARP VSTVVDDRSQ ATYGQLPTSP
FAPDLAPDVA LTGAMDLSHF IDLSSLPDAP VDAASDAAFE TDTSPVEAPS VADAAPAVPA
LPESGDTPWF DIKLDYRAEP RWSESAVPVT DATITLGAPL NVVPPPALPG DVHAGADFDP
APAGDALEAH AWHDASVDVE ALSSDAVLPT AGDDQPVSSD IEFADAPPVS SEALEAAPSH
DDAPDFSNLD QADLDATALA STDAEADVSG VSLTEPEAAA EAMAWAERVD AADTTGITSG
FDAAPAAPES TPQAASETET EAEAEAEAEA FTEFSVAPEA EQDTPSAQDG VDLPPTPAAT
EAPAMAEQML DFTLIDRDLV DIFVEEGNDL LDHSDGLLAR LRNAPDDRGL VIGLQRDLHT
IKGGARMAGI EAIGDLGHAI ESLLEQIAEH RADVDRGVIA LLERGFDALH GMLARTAAYH
VATPRPDLVA EFDARARGEV IAAPDAVTFE SEAEVPPALV EFDDGAASFA EPVEAAPAEP
DAVPHAPSED APQVFEIETI EAAAPPEDDA ASNADDAAVE RSKEIAQDDA LQIEDVAETT
SFELAHEAPA TDELADEASA PEPELTLEPE PDATPLGGIG LESPLSLEDL TPAEPFEDVE
EISLPPVADA PADSAEPAAP VFEIEPAPEA LAASASSNDY LDADLLAALD AALGTSYGAA
AKAQQTGEPI AFSEEAAQDA TPTDAFELAA QTDVADESPA SIEPEVAFEP EPEFEAEVSP
EPVPPPVPAF LAPVVAAPAV VPQPVAELPA LSAPIDMQLA GDDEHSTLST GQEQVRVRAD
LLDQLVNHAG EVAIYRARLE QQMGAFRAAM AELDRTNTRL HDQLRRLDLE TEAQIVARYQ
REQDTRDTAF DPLELDRFST LQQLSRALGE SAADISGLQT VLDDLARQND SLLGQQSRVS
SELQDGLMRA RMVPFEGSVP RLRRVLRQAA GDTGKQAQLQ LEGAHGELDR NVLERMTAPL
EHLLRNAVAH GLETPQARRE SGKPEEGVVR VVLRREGSEM VLQVADDGAG IDHAAIRRRA
EQRGMLPAGA ELADIDLERL ILEPGFSTAE EVSQLAGRGV GMDVVHNEVR QLGGSLEITS
TRGQGTAFTL RLPQTLAVTQ AVFVQIGETQ FAVPVAAVGG VGRISRERFE AADAAYVYGG
EEYALHDLGT LVGQGPAKAE GQPQIPLLLV RAGELRAAVA VDQVLGNREI VVKPVGPQIG
SIPGIYGATI TGDGSVVVIL DAAPLVRRFI AQPALANASV APAEQRHVPL VMVVDDSLTM
RKVTSRVLER HNLEVSTARD GVEALERLEE RVPDLMLLDI EMPRMDGYEL ATAMRADPRF
AGVPIVMITS RTGDKHRQRA LEIGVQRYMG KPYQELDLMR NVYDLLGMAR VRD
//
