ID B0RQ46_XANCB Unreviewed; 2332 AA.
AC B0RQ46;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=pilL {ECO:0000313|EMBL:CAP50581.1};
GN ORFNames=XCCB100_1233 {ECO:0000313|EMBL:CAP50581.1};
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169 {ECO:0000313|EMBL:CAP50581.1, ECO:0000313|Proteomes:UP000001188};
RN [1] {ECO:0000313|EMBL:CAP50581.1, ECO:0000313|Proteomes:UP000001188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100 {ECO:0000313|EMBL:CAP50581.1,
RC ECO:0000313|Proteomes:UP000001188};
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorholter F.J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O.,
RA Linke B., Patschkowski T., Ruckert C., Schmid J., Sidhu V.K., Sieber V.,
RA Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puhler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP50581.1; -; Genomic_DNA.
DR KEGG; xca:xcc-b100_1233; -.
DR HOGENOM; CLU_000650_0_0_6; -.
DR Proteomes; UP000001188; 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; 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; 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 Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 724..831
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1561..1665
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1822..2055
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2057..2190
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2209..2325
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 525..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1240..1265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1927..1946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1931..1946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 771
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1608
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2258
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2332 AA; 249700 MW; 206D5DD0C2F3A9EA CRC64;
MSALRDAMSH AALGWVKPEL DETLRQARNE IEYFAEEPSD TSRMRFCAGY LHQVQGTLRM
VELYAPAMVA EELELLANAV QAGEVSDRDE ACAMLMRGTV LLPDYLERLQ NGHRDIPIVL
LPLLNEIRAT RGQPGLNESV LFAFDPQAGV ATEAELDHAR GSLSGRNREL LDTVGNAVKE
ELLRVKDALD LHLRTGGDIA ELQTQVKELG SVADTLGMMG LGVARNVVVQ QRDALARVVD
GQVQMDEGVL LDIAGALLYV DASLDDQVAS LGADVGEAGD EASTSASASE VRRTVDVLAQ
EAIANFGAAR EHFVAFIETN WDHARLTDVP HLLGEVGGAL RILELPQAAD YLEGVRRYVD
LELIGKQRVP SGRQLDTLAD AMASLEYYLE ALRERRPGRE EILDITRNSL ETLRYWPLPS
GQPSELPVGA DQPGAAEPQP AVVPFAQQLS EPNPAANDAA PAASLEWANE TVHEAPFADS
AVQDTGAAAT DSVFSFDPVA AEETVSGQSH VPFTIAPVAL SDDGAQAPGS WQLDTTEQSA
PPTLSAFDPV SAEQDGSDAE AAQVSYTVDL SALEQDVPVV PVVAEEAPLQ IEQIDLPGED
TIAPLEFITP VQSQRAGSLE DAFSPPPPQE DDNPFVESAP EPTPEPSEPT PEAAGPRVQQ
ATVSEFELDD ASAAFLAQLD AAAQQLDVDG APATPATADA AATPVPDAPA PVAAEAGIFG
GFGDSDIDDD IRDVFLEEFD EELVNLGQLL PVWRAAPHSQ ENLRPIRRVF HTLKGSGRLV
GASTLGEFSW KIESMLNRVL DNSRPASPAV VAMVELAYAV LPQFNAALRD QGRISADLPD
IQAVAERVAA GEEAYYVPAV QAVAEAPVIP ALPAGTPPIT EGTPASVDSV LREILEAEVA
THLETVHGWL QAAQHGPQLV TEELLRAVHT MSGAFAMTDV PEITLVTTPA ESYVKRLLGA
SATPSAEGVE ALAATAAAIA TTVTALRADA PLIPSFAPLT ERLRGLVDEL PEAQWPPQVF
LDELEEVDAA QDTAGIELTG VEDLSRYVNA DALATTGDVS AQAAGDAALD AQPQDDAPTA
VDELATAEAD DSSALSLDDA APREAISDTA ELEQQLREAI DAVPMSADAS LENTQQADSD
ADAELTTAQD TVADEPVLAA DAWDATDLQT TAPAAVDAHA GDRTYEDAAT DRAADEAEHT
AHAETEAATF AASDAVAVDE LAEAEARLGD AQTLDVPSLD EAPAEQHASS DLQAEQGEQP
SEQTHADADA LGEHAEQQDQ DRDEHAADTS VETIDALEAV HAGTDANDGA YAPVAEEWTP
ETAALDSVDT THAMQDSGQQ QEQHELPHDH VQPSEHFDAQ DGDAGHDHDQ QVADEAALLA
VDGAQPLDAF AASSETDAAQ LDDAPLEHAE AGDSVPAQTI ESVQAFEMAQ VADRVEQASD
PLADTLPSEA IADVAPAQDA AAGDADSSND QVADDADRSS DQGAAQLHDT TRDAQDEHVE
HAEHVEQVAQ EEPAVTAEDA AASAEEDTAP VAFSAPVEEA APADTTANDA GAAFDIGPLN
FDELDGELVD IFVEEGRDLL DHCDGLIARM REVPEDRDVL NGLQRDLHTL KGGARMAGIN
AIGDLGHAIE SLLEAVAANR TDIDRDDVRL FERGFDRLHQ LLTRTGMHRA VAMPVDLVEA
FETRTRGRST APQTDADVRA IAKASVEPAP LSAPIPVDGQ VEEDFLPRVQ QEQVRVRADL
LDRLVNHAGE VAIYRSRLEQ QLGAFRGAMG ELDRTNARLR DQLRRLDLET EAQIVARYQR
EQDQGDRTFD PLELDRFSTL QQLSRALNES AADLGGLQGV LEDLSRQYDG LLQQQSRVSS
ELQDGLMRAR MVPFDGLVPR LRRVVRQAAT ETGKQVHLVL EGTQGELDRN VLDRMVAPLE
HMLRNSVAHG LETPEQRRDA GKPEEGSIAI RLRREGSEIV LEVADDGAGL DREAIRRRGE
QRGLIEPGQE LSEAELDGLI FASGFSTFDQ VSQLAGRGVG MDVVRNEVRQ LGGSVDIHSV
RGQGVTFTLR LPQTLAVTQA VFVRIGETTF AVPVGSVSGI GRISRTRYES GEGGYHYAGE
EYVLHDLGSL VGQPVARADG QAQVPLLLVR AGDLRAAVAI DQVLGNREIV VKPVGLQIAS
VPGIYGATIT GDGRVVVILD VAPLVRRYLT QPARPALETP AEAQRQVPLV MVVDDSLTMR
KVTSRVLERH NLDVTTARDG VEALELLEER VPDLMLLDIE MPRMDGYELA TAMRADPRFK
AVPIVMITSR SGEKHRQRAF EIGVQRYLGK PYQELDLMRN VYDLLGIARV RE
//
