ID A0A1G9D0Q6_9GAMM Unreviewed; 2001 AA.
AC A0A1G9D0Q6;
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=SAMN05216212_2699 {ECO:0000313|EMBL:SDK57528.1};
OS Microbulbifer yueqingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=658219 {ECO:0000313|EMBL:SDK57528.1, ECO:0000313|Proteomes:UP000199305};
RN [1] {ECO:0000313|EMBL:SDK57528.1, ECO:0000313|Proteomes:UP000199305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10658 {ECO:0000313|EMBL:SDK57528.1,
RC ECO:0000313|Proteomes:UP000199305};
RA de Groot N.N.;
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; FNFH01000005; SDK57528.1; -; Genomic_DNA.
DR STRING; 658219.SAMN05216212_2699; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000199305; 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; 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; 6.
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:SDK57528.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SDK57528.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 617..724
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 775..880
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1169..1275
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1479..1712
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1714..1853
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1879..1995
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 557..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 664
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 823
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1216
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1928
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2001 AA; 218972 MW; C783F01D73422F8E CRC64;
MSHDNPNFEA LDWLTGEINE TLAQARHALE SYANEGAAEP DKLQACLELI HQVHGSLHMA
ELTGAAMLAE EMEQLIQALS TDEVENSEET REFLMRALLE LPLYLDKVAY QRRDNAVLLL
PLLNDLRAVR RERLVTEGAL FSPDLSALGQ AHGARQPLVA DSARLQELVN KLRKMYHVAA
AGLIRDVNGG DSLSYLRKVA EKMQLLYSGS VRQPLWQILE GLLEAIGEQR INVLPALRQL
LRRIDVEFRL LQGRGAQVLD APLDRGLVRN LLFYVYMAGP NSARCKSLYA TFALDRAVPG
TPRPDTGEAL AMGPEAMGTA IKALREELDG VREALDPTIT GEEPASLSDI ATVAQRIADT
LGVLGLESQR LRARGIYESL RDASRTDDPQ ELLLQAASEV VQLDSSLASA LNRQHQGHSE
QPLMGDATDS VLREARTGLE SVKEAVVEYI ASHWDVSHLH RVPERLQEVG GGLDMVGFQR
AGDIVAACTR YIRERLIEAA EQPEWKVLDT LADAITSVEY YLERRAEGIE DADMLLALAE
DSVSALGFGV DNREVAPTGA VPAEPAPQEF AATEEPEEFS PESIAPAPAE PESAPGETGT
PQAAEPEPAQ VADDDDENLI DEEILEIFLE EADEVLETIR EFFPRWAADF SDRAALVEFR
RGFHTLKGSG RMVEALDIGE LAWAVENMLN RVIDETVKPQ RGHVHLIEHV CAKLPSMIDA
FRAQAADPDP ERTEQLRAWA EQLAHGESPA DLDAPAVADS GAAASPAGGA ATDDDSDDNA
QLWEIFAQET ETHLATLDEF LADMRAAAPL YGVPSDPLHR ALHTMKGSAH MADVTPVAEL
VTPLERFVKE LRTYQVNIDE DIYELLEDGA TYVREVLDQI RNQQPIHIAK AEPFLARTAE
LQERAVGHLI RERESSEPRE VDPQLLAVIM ADGMKVLLDA DEVLGAWRRE PANTGLLEPI
AEELRVLEEA AQRAQLPTLA ELSRLLLEVY ARILDNTLEG EPALWASLEQ GHSELLDLVD
AVAAAQDLPD VSDAVGEALR ALAQGESASE EEDFDWAELG IDHTDLPISY STPDGADERS
ADAGDTGSDD PAVTDDWAAL ELDSTDLPTT HQQETGYDLS GQDQAADLGL DESLLGGDGP
ASEAGAGDNR QPTSAPDSPE TAARDNTPVA DIDPDVVDVF MEEAGDLVDE LEELIQGWEA
DPADYSRAEA LKRVLHTFKG GARMAGLMGL GEVAHRFETV IEAMPSSDHP GPDFFANAHG
IYDRIAGGVE TVRAWMAGDE LEAFAELLDT AWADSQVAET PEAAEPAPVV DDELQPDDGG
AAADETAPQD EIAPQPEGEA ATPALLGAVD TKPVPLAPAE AASNVLPFVR KKDSLHPNEQ
RGGNRGQPQE MVRVAAELLE ELVNLAGETS ISRSRLEEQV SEFGFALDEM DSTITRLNEQ
LRRLDMETEA QILFRQEQLA EQDDNFDPLE MDRYSSIQQL SRSLLESTSD LLELRNTLGN
KARDTETLLL QQSRVNTELQ EGLMRSRMVP FSRLVPRLRR IVRQVSAELG KQVDLVFSNV
EGELDRSMLE RMVAPLEHML RNAVDHGIEL PARRQESGKP ERGRITVALE REGSEVVLTI
GDDGAGINLM KVREKAIERG LMRADAELTN NEILQFILQA GFSTADRVTQ ISGRGVGMDV
VSAEIKQIGG TVHIDSKLGA GTEFTVRLPF TVSVNRALMV SVGDDVFALP LNTIEGIVRL
SPYELEHYYS SPDARFEYAG EPYQVNYFGT LLQSEARPKL EVEDAQLPVL LVRSEGHAMA
LQVDAVLGSR EIVVKSLGPQ FAAVQGVSGA TVTGDGTVVV ILDAHALLRQ QAALLARPAE
LALPSAPRVK PEPVETQQRV MVVDDSVTVR KVTTRFLERE GYLVNTAKDG QDAVIQLQDI
RPDVILLDIE MPRMDGFEVA RHIRGNSRLR DIPIIMITSR TGQKHRDHAL SLGVNHYLGK
PYQEEVLLEA IRDYTVAPAS Q
//
