ID A0A385YWA3_9PSED Unreviewed; 2521 AA.
AC A0A385YWA3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=D3880_01550 {ECO:0000313|EMBL:AYC31149.1};
OS Pseudomonas cavernae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2320867 {ECO:0000313|EMBL:AYC31149.1, ECO:0000313|Proteomes:UP000265560};
RN [1] {ECO:0000313|Proteomes:UP000265560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K2W31S-8 {ECO:0000313|Proteomes:UP000265560};
RA Zhu H.;
RL Submitted (SEP-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};
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DR EMBL; CP032419; AYC31149.1; -; Genomic_DNA.
DR KEGG; pcav:D3880_01550; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000265560; Chromosome.
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; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 5.
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; 7.
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:SF8; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 7.
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; 5.
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; 8.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000265560};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 821..925
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 980..1086
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1316..1423
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1590..1690
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1732..1843
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 2001..2234
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2236..2375
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2402..2518
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1447..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1482
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 868
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1026
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1363
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1633
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1779
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2451
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2521 AA; 275140 MW; 538378C784D3EB84 CRC64;
MGDRHDYVAL EWVKGEIAET LKQARQALEA FVESPQDSTR MRFCLTYVHQ VHGTLQMVEF
YGAALLAEEM EQLAKALMDG RVGNQGEALE VLMQAILQLP AYLERIQTAR RDLPLVVLPL
LNDLRAARGE NLLSETSLFS PEIASPLPQL SHESLAQLRT AELPVLLRKL RQMLQMALVG
VIRNHDLATN LGYMARVFAR LELLCKEAPL GPLWLIASGL VEGLANGSVV NGTSVRTLLR
QVDKELKRLL EQGADGINQA APDELIKNLL FYVAKAPAQS PRIRALKAQY RLDEALLDSA
EVDEERARLA GPDRDAMRSV VTALCEELVR VKDSLDLFVR SDRQRVAELD GLLAPLKQIA
DTLAVLGFGQ PRKVILDQID VVHGLSLGQR EPSDALLMDV AGALLYVEAT LAGMVGPSDD
GGREESHLPT TDVAQIHQLV IKEARTGLEQ AKDAIIEFIA SQWNHEHLAR VPELLTQVRG
GLAMIPLSRA AELLNACTRY IQEQLLARKA VPNWHHLDTL ADAITSVEYY LERLSEDHAS
QGDLILDVAE ESLESLGYPL KQKPSILDRV EPVAQPAPLA DPLQDIEVLQ DEPLDTFAPS
ESAPSEELAL PDLGGDLDFD LGELPGAMAQ ASADEALPLA ELQPLEDGWQ LVDNDSLIDF
NLDARSQAEY EALTLAALDE ALAEPVSEAE EPTELDWESA EPEAFDVVEL DLVDDTLAGL
EPLPELEPFE VGAPAADLSL ELEELSLAAL EETPPDWSTV DLSELDLPEV ELPSALPTVT
QLIEPESKPL SVAEVMAAPV QAINPPAQDV PLSLLPPPAD EEAIDDELRE VFVEEVDEVL
ETLGEYLPRW QAERDDKGAL SEVRRAFHTL KGSGRMVRAL IIGELAWSIE NLLNRVLDRS
IVPSDEVLQL VGAVAELMPA LLAEFAAKAQ RQRDDVDQLA ASAYALAKGL SLAKAEAAAV
QPAPVAEAEV AAAVGEESAG EVLDPQLIEI FRNEAETHLD TLVAFLADCA QELPQPVTDD
LQRALHTLKG SASMAGILPV AEIATPLEKL VKEFKANLLP MDLAEAELLH SAEQLFRLGL
EQLASQPLAP ILGAAELLER VQQLHHERLE AAQATRQGES NESRDPQLIS IFLAEGMDIL
LDAEDLLRRW REHPAERQEL SALLEELTTL GRGAEMAELP QIDELCEALL DLYGTVEEGR
LAVSERFFSE AESAHEALIG MMDQVAAGLQ VSAQPERVAA LRALLDEALD PRTLALLSMD
NDGGLQITEL DSATAELELA QWALDGPAAR SAGEAGGLTW DEAAFALDEP APTRIQDPLD
EEMVAIFLEE AVDILDSAGQ ALERWLAEPA NHLALSSLQR DLHTLKGGAR MAEIRPIGDL
AHELESLYEG LVDRRYNYSP ALAALLQQSH DRLAVLLEQL QGQRPLAEPM DLVQAIRSFR
QGGAASLAAA ATMPQPDCEA EAEAEAEAEA EAEAEAEAEP ALEAESESPL PSLPVVEETP
ALAVLLAQDL PEAGEAVDFA AAPDDSLPLE QEGWPEAESV AEAASDELVA PSWTEGEAVA
AAPEPAAADE PPFATPAGVA SPAPLQDERD PELVEIFLEE GFDIIDSSGA ALQRWMADSD
NTLEVESLQR DLHTLKGGAR MAEIREIGDL AHELEFLYED LGNGRLRASA SLFALLQRCH
DSLAAMLDAV RGQRPLADGN ALIEAIRHFR SNPAEQLGVP RSVQLKAVET PDEEAEADIL
DIFLEEGDDL LEEMEASIGR WEEAREDGGA IDYLLRILHT LKGGARLAGQ KRLGDLTHDL
EQHLTEAQQQ GAPWPESLFL DVQSGFEGLQ RELDELRQRL DASLPAAGVN APATEPRPTE
VGGPLPTTLA TPIIAASQAP AQVSETKVLP FVRRAQEAAQ EAAARRAPQE LVKVPAELLE
GLVNLAGETS IFRGRVEQQV SDFGFTLSEM EATIDRVRDQ LRRLDTETQA QILSRYQAEA
ERAGYEDFDP LEMDRYSQLQ QLSRALFESS SDLLDLKETL AARNRDAETL LLQQARVNTE
LQEGLMRTRM VPFDRLVPRL RRIVRQVASE LGKQVEFIVG NADGEMDRTV LERIVAPLEH
MLRNAVDHGI EPAEVRRAAG KSEQGSIRLS LGREGGDIVL TLSDDGGGIK LEAVRRKAIE
RGLMDADSDL TDYEVLQFIL ESGFSTAEKV TQISGRGVGM DVVHSEVKQL GGSMSIDSTL
GEGTRFLIRL PFTVSVNRAL MVLSGEDLYA IPLNTIEGIV RVSPYELEAY YQPDAPRFEY
AGQSYELRYL GDLLNNGQHP KLVGQSLPLP VILVRSSEHA VAVQVDSLAG SREIVVKSLG
AQFASVHGIS GATILGDGRV VVILDLLATI RVLHAHLLTQ LQPRTTHLLA PSVEVEVERP
PLVMVVDDSV TVRKVTSRLL ERNGMNVLTA KDGVDAITQL QEHKPDIMLL DIEMPRMDGF
EVAALVRHDE RLKDLPIIMI TSRTGEKHRE RAMNIGVNEY LGKPYQESLL LETIAQLVKR
T
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