ID A0A143HJA7_9GAMM Unreviewed; 2083 AA.
AC A0A143HJA7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=A3224_01035 {ECO:0000313|EMBL:AMX01352.1};
OS Microbulbifer thermotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX01352.1, ECO:0000313|Proteomes:UP000076077};
RN [1] {ECO:0000313|Proteomes:UP000076077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA Lee Y.-S., Choi Y.-L.;
RL Submitted (MAR-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; CP014864; AMX01352.1; -; Genomic_DNA.
DR RefSeq; WP_067150318.1; NZ_CP014864.1.
DR STRING; 252514.A3224_01035; -.
DR GeneID; 76606629; -.
DR KEGG; mthd:A3224_01035; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000076077; 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; 3.
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; 5.
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:AMX01352.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW Transferase {ECO:0000313|EMBL:AMX01352.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 662..766
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 817..922
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1263..1369
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1590..1793
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1795..1934
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1960..2076
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 628..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1419..1447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 709
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 865
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 2009
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2083 AA; 228356 MW; 2FB81B33C073EE75 CRC64;
MSHDNPNFLA LGWLTGEIND TLAQARQQLE AFASASTEGA SAADNGLLKH CLELIHQVHG
SLHMAELSGA AMLAEEMEQL VQALAGGEVE NSDETREFLM RALLELPLYL EKVSFQRRDN
PILLLPLLND LRAVRRERLI TEGALFAPDL SPLEQVRGKR QALTGNNAKL QELVGKLRKM
YHVAGAGLIR DVNSKESLAY LVKVAEKMSL LYSGSVRRPL WEILLGIFEA VAEHRISVMP
ALRQLLRRID VEFRLLAGRG AKVLDARLDR DLVRNLLFYV YLAGPNGPRC QALYQTYALD
KAVPGTPRPD TENALAMGPE ALGTAVEALR EELRLVREAL EPETASTERP PLSDTAAIAK
RVADTLGVLG LENQRARART VYECLRDAAR GQDVDELLLR AAGDLVQLDT ALASTAARNK
QVNDDQPLMG DATNTVLREA RLALEVVKEA VVEYIASHWD ISYLSRVPER LQEVCGGLEM
VGYQRAGKIV DACKRYVSER LIEAEEQPEW KLLDTLADAI TSVEYYLERR SDGIEDADML
LALAEDSVAT LGFAVTDEAL EIEAEPLSVG DAATADETEA TADFIAELPD EPVQEPISAA
ETTAVEEGDY TAELQLAGTQ PTAVETVEFE SESEPDTTLS ADADAHAEPV ETAPAASLDD
DDNLIDDEIV EIFLEESAEV LETIGQYFPQ WAANFGNRDA LVEFRRGFHT LKGSGRMVEA
VEVGELAWAV ENMLNRVIDD TVQPTRAHVE LVEQVRRKLP SMIEGFRLRT GDPDPQRTAQ
LEAWAQQLAN GEEPEDLLAA SESQMPEIPA AEEAADAGED IDQLWEIFAQ EAETHLAVVD
EFLAEMRDAA PLYDVPSDPM HRALHTLKGS AHMAEVTAVA QLVAPLERFA KELRTYQVSI
DADIFELFSD GADYVRRALE QIRAGEAPVI EKSEQFLARV AELQERSVGQ MIREREANQP
KSVDPQLLAV IMADGMKVLL DADQMLKQWR SNPADKSLLA PVAEELQVLE EAASRAQLPT
LAELSRLLLN VYRKVIDGRL EVEPALWSAL EEGHSELLDL VDAVAAAQDL PEVSEAVGEA
LRYLAQGDNV SSEEDDYDLA ELGIDSTDIP VAQAEEEVPV ASVAASDDSG DWGLDGLLAA
EADHMPATED EQRTTPAAEE NAPVPPVAEA VEPAAVITTE EVGGLDTDGR DEAGVFGDLS
FDDLLIADGQ SSAPSAVEGS ETPLEEQVTP AAPMAEEPAS TVAEVRQPVA DTSPSDDELQ
KLLADIDPDV VEVFLEEAGD LVDELEELIQ EWEQAPADQS QAEALKRVLH TFKGGARMAG
VMGLGEVAHR FETVIEGMQG KAEPSMEFFA DAHAIYDRIA AGVETVRAWM GGEQLDAFAQ
LLSTTWADAQ MAEDAAPAGY QETPEVTPVL DEPRQAAEIT DTTPEPPAEQ PPQAVPAPRD
EPPSNVLPFI RKKAGVSERE SGAGVRSQPQ EMVRVAAELL EELVNLAGET SISRSRLEEQ
ISEFGLALDE MDSTLQRLNE QLRRLDMETE AQILFRQEQL AEQDDDFDPL EMDRYSSIQQ
LSRSLLESTS DLMELRATLG NKARDTETLL LQQSRVNTEL QEGLMRSRMV PFSRLVPRLR
RIVRQVSAEL GKQVDLVFSN VEGELDRSML ERMVAPLEHM LRNAVDHGIE APEVRAAAGK
PERGRISVAL EREGSEVVLS ISDDGAGINL MKVREKAIER GLMRPDAELS NNEILQFILQ
AGFSTADKVT QISGRGVGMD VVSAEIKQIG GTVHINSQAG QGTEFIVRLP FTVSVNRALM
VKIGEDLFAL PLNTIEGIVR LSPFELEHYY RTEGAHFEYA GEPYEVSYFG TLLKSGARPK
LDGRDMQLPV LLVRSEGHAM ALQVDAIMGS REIVVKSLGP QFAGVQGVSG ATVTGDGTVV
VILDPHALLR RQAAQLARPD VAKLESKPQV LPEPEERQLK VMVVDDSVTV RKVTSRFLER
EGYLVTTAKD GQDAVIQLQD QIPDLILLDI EMPRMDGFEV ARHIRGNQRL RDIPIVMITS
RTGSKHRDYA LSLGVNHYLG KPYQEEVLLE TIREYTGEAA ASG
//
