ID A0A1U6GQ58_9GAMM Unreviewed; 2315 AA.
AC A0A1U6GQ58;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=cheA {ECO:0000313|EMBL:SLJ85580.1};
GN ORFNames=DABAL43B_2396 {ECO:0000313|EMBL:SLJ85580.1};
OS Psychrobacter sp. DAB_AL43B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1028416 {ECO:0000313|EMBL:SLJ85580.1, ECO:0000313|Proteomes:UP000190084};
RN [1] {ECO:0000313|EMBL:SLJ85580.1, ECO:0000313|Proteomes:UP000190084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAB_AL43B {ECO:0000313|EMBL:SLJ85580.1};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; LT799838; SLJ85580.1; -; Genomic_DNA.
DR STRING; 1028416.DABAL43B_2396; -.
DR KEGG; psyc:DABAL43B_2396; -.
DR OrthoDB; 9803176at2; -.
DR Proteomes; UP000190084; Chromosome i.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00088; HPT; 3.
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; 5.
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; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 5.
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; 5.
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; 5.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000313|EMBL:SLJ85580.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Transferase {ECO:0000313|EMBL:SLJ85580.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 622..726
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 841..945
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1040..1143
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1343..1450
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1521..1624
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1772..2025
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2027..2169
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 2189..2305
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 439..466
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1739..1766
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 669
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 888
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1086
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1390
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1567
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 2238
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2315 AA; 258115 MW; 29CDF63A98B82F2B CRC64;
MNNQPNDMVT IEWLLPLFNQ QLSQVADGWQ LGAENSNYEQ TAQHYHQISG ALTMINLPSL
ASLATKLSLL VEASNPQDLN DNVNNLDSSL NDDSFDTHFA AEKARVGQVA HRLLQHELVH
YARTGNYHSA LINKVSAELT QALSRFDIAT DHLIDSVLLS AASDLDSRSD HDDIDITIPA
SMAVSDLDSQ QHQQLLLVWR QQVQELLAAN VNKPSILTVL EKVSQYLWQT AQAADLQRLW
YLTELWLHDL GKNESPLPMH YAGLLSQLDQ VIESYQHQTE LSTSAIKKLI SSIYIELNGL
VNHSDNTQSI LSGWSQADTE SRFLPRILNA IEAIIFSLDK PHNLLKPLQK ISAQLEGHGW
TLYASQVTSI LADIEHNLSS DKDFAQEQWQ IERQLQELYS AIYNTEQIIS TKIGSAASFT
SLSQVVASDD LQPESSTYIS ANNEDLRELR IAVEEIKQDF HDYIQRQDTD LLPDQADFTR
MSHAFDSMGL PSIGQATDKI ADIFVQIHTH GIEALSWDVT QALAEGLTSI ELLLDYLAQQ
FFDQSLLEKA NGYIDKAATL LSEYIHAPET VNDTFLTQKT AATDVLRYDD SGEISPIIDQ
SFVADAVSDA LLRARHQLKA DNFDIDEDIR EIFIEEVEEV VADLEDFLPI WQEDVQDLTP
LTEVRRGFHT LKGSGRMVGA FSISEMAWSI ENLLNRLLDK TLPVTDDVVA LVTETTKRFP
AMLGDFKAQQ TPSFDPAITI LQSHNLMTQQ PLNFGLETAE LAFSKPEIEQ DSAISDHSVS
GHSLHSQASN LTVETASSID PITTIKDTGE ARNLSELLAD LEIPLVLKSF ISESTVLAAD
ANDADPDIKE IFIEEANEVL DEIVPLYEYW RLSPSDLTGL TDIRRGFHTL KGSGRMVGAN
YSAELAWSIE NMLNRILDKS ITASTDIQQL IGDVLAAYPA LLTTFENESE DYPAMLPLWV
ACANAYSKQL GDEFSYNVLY GQLASPAEQQ VSGHVTLHSG LDNHAQDSDN GSDETIDHAL
QTIHSVNEKM AEAPIILTPQ SEEEQAFFDI FIEEAEELLE GINEFVSSHQ DESHVAVSDE
IVRAFHTLRA ASGSSALAAI SDVSATIEQS LELLQQQDIP MNAKHLSALA QSVTLINGYL
DNYKQNAQQQ DMSIEDMQSE QDIASLQALL GKQNVDDAGE AIADDKPTIN QLLDGDIDDL
LDAEWQLAEA LSNSEIDQVQ KYITQQIAQI KYLTEKAQVF PKFTSILHAL ENAYNYLSKH
VEKSANPEIQ AILLAGHAQL IGLFDALAGS TSLKIDEQVL EQLQNISQHN DYSDQNDAVV
AHEAYEDGAA VQSIAAPELQ LESIDTDIEL LEIFLEEAQE LDDALVDSFS KWRADITNIN
TLKVLQRHLH TIKGGARMAG IRSIGDLTHE AETIYEAFVE VRRTPTVQWL EIMQVVQDTL
SLQVAHIVRY QKSFFAPELI EQLQQFEKAK ALPETVQLIV PMPKNHVDVE SKVHANEYTH
RIEKAADTLS LDRIIKQSWA HGLPDPDILE VFLEEAEALT NRNEYLQLFL SDAGDMIALQ
GLQRDLHTLK GGARMVTASG IADLAHEMES VYKDFVDRRR PATKKVLELL VACHDWLADA
VFILSQQVNP PTPDLLIEAL QQFSKNPDSL KQIPKETLQP QREAILIAKE KQETTYIQKD
ISDMPLMVSD VAEHEQNANN NEMIRISGGL IEHMINLSGE STINRARIDM GISSLTNSIE
EMGTTVQRLA DQLRRMEIEL EAQILSQIDD ELVNHEGFDP LEMDQYSSLN QLSKSLTESA
SDLVDINHTL LEKTRDSESL LLQLSRTQTE LQDGLMNSRM VPFTRLTPRL ERIVRQTANE
LNKSVELKII NADDEMDRTI LERITSPLEH MLRNAVDHGI ENASTRLEAG KERSGQITLE
VLREGSEIVI QLTDDGYGID VEAVRNKAIS QGLIDADDSS LSDLDIMQYI FNAGLSTSKQ
VTQISGRGVG MDVVISEIRQ LGGSVSVISE LGKGSRFTIR VPLTVAVSDA LVVRAADRYY
AIPLVQIERV VRINPEKIYD YYQSGEATLN FEDTDYRVRY LNEILSGNKL NELVVNTNTS
VPLIIIKNRS GQNMALQVDQ IAGSRIEVVV KPLGQQFSNL SGISAATIMG DGSVMLILDL
IALMRNAALV KEVSQPAIVK RRSSESKGTI LVVDDSVTVR KVTSRFLERQ GFNVALAKDG
IDALEILQEM TPDLMLLDIE MPRMDGFEVA TQVRHNRRLQ HLPIIMITSR TGEKHRERAL
EIGVNDYMGK PFQENQLLDK IQSLLDKKVS LTHDG
//
