ID J2L5B8_9BURK Unreviewed; 2075 AA.
AC J2L5B8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMI15_01174 {ECO:0000313|EMBL:EJL87480.1};
OS Polaromonas sp. CF318.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Polaromonas.
OX NCBI_TaxID=1144318 {ECO:0000313|EMBL:EJL87480.1, ECO:0000313|Proteomes:UP000007275};
RN [1] {ECO:0000313|EMBL:EJL87480.1, ECO:0000313|Proteomes:UP000007275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF318 {ECO:0000313|EMBL:EJL87480.1,
RC ECO:0000313|Proteomes:UP000007275};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL87480.1}.
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DR EMBL; AKIV01000039; EJL87480.1; -; Genomic_DNA.
DR RefSeq; WP_007864992.1; NZ_AKIV01000039.1.
DR PATRIC; fig|1144318.3.peg.1122; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000007275; 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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 3.
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; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 3.
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; 3.
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; 4.
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:EJL87480.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EJL87480.1}.
FT DOMAIN 690..794
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1026..1129
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1263..1375
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1531..1764
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1766..1902
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1951..2067
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1156..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1465..1506
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 737
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1072
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1310
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2000
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2075 AA; 221711 MW; CC7B4104AF45B72B CRC64;
MQSNVPNSTA AELDLAVNDL GPLAWVLDEL RKSLDGAAKA LKRFVRDAEA ARGSDLAAVD
ASQLRIARQQ LHQAVGALEM VGLAGPALVL RAMEAAVQKF VQQPEQCSQE AAGKIERASF
ALTEYLEGVL ADKPISAVSL FPQYRDVQEL LRADRIHPAD LWSFEWRWLE PELTGTSEPR
NYDDSARAVL DQSVLQIMKG KAPQAAKSLK ELSLGFAARQ ADRQPRIFWK VAAAYFEAVA
NDLLGSDLYV KRAASRVLMQ YASLAKGDTS VSERLAQDLL FFCSQAVSAR ASDTPVLSAV
RSAYGLNRFK PVDYELIQFG RFDPALLAQA RKRITSAKET WSALSAGDAN KFKSVSDQFS
LVTDSLLKLH PPSEPLAQAL SRAVETVVRS GQAPGIELAM EVATSVLYLE AAFDDLDPND
PQLAVRTANL AERLEGVRAG GQPQPLEGWM EELYRRVSDK QTMGSVVGEL RVSLGELEKS
LDVFFRNPQD KVTLQAVPGQ LSQMRGVLSV LGLDQASHAV LRMRDSVEQM LVTEIDEQQA
RAAGTFEHLG NNLGALSFLI DMLNYQPALA KKLFVYDDQK GELRPLMGRV QNAASAASAV
TVGGDMLSQE VIAVVQDAGQ GEADASLTIK LDALATHAAL AEQPALAQTA REAAVAVSTS
DTDAAATALT TLAFTVAPAP AAPEPAAESD DFEEDDLRDI FLEEAREVIG NGREALAALA
TDPADVSQLT VLRRAFHTLK GSSRMVGLNE FGEAAWSLEQ MLNTWLADQK ATTDEFRALS
TEAMGGFADW IADIAANKDG AWSASVFRAS ADAMRTEGRY SPLVLGAKAA VAAPAAAPPA
AVADTAPAAE PAATEAFSLP DFELDAGAPE AASAAPAEAT APLTDLDFDL VFGDAAPAKP
AEPAAEIAGI DFDSLSAISG DAGVPAQPVA AADAATVIEL DSAEAIELSD ADFDKHFHAE
AAEPVKADLA DDLNFDFSAT PPQAAAVSEP APGQPQVEAL DALDRVEATD SAMSVDGDEQ
VKVIGTLRIS IPLYNVYLNE ADEWSRRLVT EVAEWSLERN QPVSDSTVAL AHSLAGSSAT
VGFDALSEMA RALEQALQQS RAHHRNGAAK YGQVFVDAAE DIRRLLHQFA AGFLKEPDAG
VLDRLKQLDF SDSVLPPGTD FSEYDFESES VLPQEPAVEP EPVPEPEPEP VVMQVVEEAP
LIEVPAPAPA PTPAPAPVQA APVPPPVGFA APPVAVAPPV RLATPAPATQ GFEDEEDEEI
DAVDAIDPDL FPIFEEEGAE LMPQLGGALR QWSARPDNQG ARMEVLRALH TLKGSARLAG
ALRLGEMAHR IESEIEFLGS DAAASAEFDA LINRFDAMEA AFEALRNADA AAAAAPVQLA
PLAAAQPEPV SAPVQAATGP DAPEAAAQSP APATAAAGGS RKLSVPAPQA MAMQPLRQAA
NASIRVRSQL LDRMVNQAGE VMITRSRLEA ELSQLRGSLN DMSGNLNRLR QQLRDIELQA
ETQMQSRLAQ AKEAQAGFDP LEFDRFTRVQ ELTRMMAESV NDVATVQRTL QRTVEATEDD
LIAQARQTRE LQRDLLRTRM VEFEGISERL YRVVRQASKE TGKQVKLDLL GGTIEMDRGM
LDRMTPAFEH LLRNCVAHGI ESTEVRTNAG KDPVGVITVH LRQEGNDVSV DFSDDGAGLD
LRRIREKAVS LGMIAPDQAI EDSDAANLIF MPGFSTAAQV TELAGRGIGM DVVRSEVNSL
GGRIETSTVA GKGTHFKLVL PLTTAVTQVV MIRAGNLSVG VPANVVETVR RASAKELQQA
YNTGTLEIAG ETMPFFWSGA LLQASQHSGE VQGKTTPVVV FRSAAQRIAL HVDEVLGNQE
VVVKNLGPQL SRLPGLAGMS VLASGAVVLI YNPVALASVY GQQARAWSTD RAEPHMLEGS
GATAASTATG TGAGGVAKAP AAMPAAPQIP LILVVDDSIT VRRVTQRLLQ REGYRVTLAA
DGLQALERLQ EERPAVVLSD IEMPRMDGFD LARNIRGDVR LNNLPIIMIT SRIAEKHREH
AKELGVDHYL GKPFSEEELM SLVRHYCAAE TAISA
//
