ID H1G1W4_9GAMM Unreviewed; 1800 AA.
AC H1G1W4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ECTPHS_03854 {ECO:0000313|EMBL:EHQ51801.1};
OS Ectothiorhodospira sp. PHS-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Ectothiorhodospira.
OX NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ51801.1, ECO:0000313|Proteomes:UP000005314};
RN [1] {ECO:0000313|EMBL:EHQ51801.1, ECO:0000313|Proteomes:UP000005314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ51801.1,
RC ECO:0000313|Proteomes:UP000005314};
RA Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA Hoeft S., Oremland R.S., Stolz J.;
RT "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT oxidoreductases.";
RL Submitted (JAN-2012) 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:EHQ51801.1}.
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DR EMBL; AGBG01000006; EHQ51801.1; -; Genomic_DNA.
DR STRING; 519989.ECTPHS_03854; -.
DR PATRIC; fig|519989.5.peg.772; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR Proteomes; UP000005314; 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; cd00731; CheA_reg; 1.
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; 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; 5.
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 Kinase {ECO:0000313|EMBL:EHQ51801.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:EHQ51801.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 684..788
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 829..933
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1002..1106
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1281..1514
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1516..1654
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1674..1790
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 605..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1131..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1004
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 731
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 876
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1049
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1723
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1800 AA; 196527 MW; 45078DAAF44584A6 CRC64;
MMITGTGWTM TVDSQQLTAL RWVKKELDAL LTEARAALET FSDDAGRTDS LEEACRLLDQ
VEGTLRMLDL HGAAMLAREM SALVGALLAG EVTGREEALE TVSRAMLQLP DYLEHLRTGH
RDVPLVLLPL LNDLRTVRKA SLLSETVFFF PDLASISARP LEEPLLPTEQ GVDIQTLARV
YRHQYQLGLV SLLRGAQIEA GAQRIDKAVA GLRRCARRAE VQRFFWVVGA ISEALRSGGL
EPGAAVKQLL GQVDRQIRFL IENDESTMAA GIPDDLLRNL LYYVGRATSR GPLVTAVREA
YRLGELLPDE AELRAAQEGL SAPNRELMLT VSQAIREDLA DVKDNLDVFM HTGGRQREAL
LPLVGKLRSM ADTLAMVGMV EPREIALREA DILEAIMNGD TAPEEAVLMQ AAADMINMEA
AIRSAAEGRG DEGGEDGLPG TLGALSPTES RALMHSLMGE ALADLARVKD AINTFVHDPG
NTAVMGEVPR TLDGLSGVLA WLNLTDEVTL LQGLRDMIQA RCIDDPRPLQ SDEETPLADV
LTALECALEA RTSGHGNADD LLARGHAALA RLGGAADAVE ASPFPDALPL DDLPELEPLP
ELSDDIQWEP LPGLEPSADH DEDVSDHTLR LELPEDDLED DRTLVIPQRV PEFEDLEPPP
ETAPVVPAME DDDDGVGGGL GALVEDLDPD ILEVFLEEAD EEVARIGEQL PRWCAYPEDQ
AALVTLRRSF HTLKGSGRLV GAQLLGEFVW ANENLLNHLI DGQVAPGPEV LAAMEASSGM
LPHLVAQIRG EPCSVADARS LIGRLQALVE RQPVDIPPAV EAPEQSEPVP RMDPVLLSIF
GAETRQHLRT LEALLDEIPS PVAGLPIQSE LLRAMHTLNG SARTAEVPEI SAVCGACERY
LNLRAEAESS VPPEALPDLR ALTVHVHGVL DALERGDASL PTAEALEARF RQLHEQEQAR
QDAPRQAWDL EAAEPADDAP PEAPVDLDIL DSEPEPEPDL VTDEPDPELV ALFLEEAVDI
LHAADASLEL WSESLGNPEP VQAFQRQLHT LKGGARMAGM VPIGDLSHAL ESLMIALTEG
ERAPEASMIE VARQALDQLN TMVEQARQGE TVVPVPRLVA RLHALIEGGE AVSIAEPSPP
PAAEPEADTE IRRRPILERA AEPVIPLRVE AEPPRPTPEP ARTGAAGQDV VRVRADVLDS
LVNYAGEVNI YHARMEQQIT SFGFNLGELE QTIQRLREQL RKLEMETEAQ ILFRHEQEQG
EARWQEDFDP LELDRYSNIQ QLSRALAESV SDLSSIQGLL ADQVKDTETL LLQQTRVSTD
LQEGLMHTRM VQFATIVPRL RRIVRQTASE LGKRVELEVE GEGSELDRSV LERMLAPMEH
MLRNAISHGI EAPDRRRAQG KDESGQVRLH MRREGSEVVL EVADDGAGVD LEAVRAKVTR
LGLSSDPSLL TEQDLMQFIL ESGFSTASQV SQISGRGVGM DVVNSEIKQL DGVLSIDSTR
GRGTRFTIRL PFTLAISQAL LVQTGDEIFA VPLSSIEGIL RMQGRDLAAF HAADDPVYEY
AGNTYEVKHL GALLKVSRPL IPSPDAMCPV LLVRSGDHRI ALHVDALMGS REVVIKPVGP
QVSRVKGIAG ATILGDGRVV MILDVPALVR AGAGVRLAYH DAQPDTASER RRGVVMVVDD
SITIRKVTAR ALERQGYHVL TARDGVDALA QLQEQVPDLM LLDIEMPRMD GFELATHIRN
DARLRRLPII MITSRTGDKH RQRAMEIGVN RYLGKPYQEM DLLTQIREVL DEHQGSGGAA
//
