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Database: UniProt
Entry: A0A2S9I909_9GAMM
LinkDB: A0A2S9I909_9GAMM
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ID   A0A2S9I909_9GAMM        Unreviewed;       909 AA.
AC   A0A2S9I909;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CQW29_16985 {ECO:0000313|EMBL:PRD14267.1};
OS   Pantoea coffeiphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=1465635 {ECO:0000313|EMBL:PRD14267.1, ECO:0000313|Proteomes:UP000239181};
RN   [1] {ECO:0000313|EMBL:PRD14267.1, ECO:0000313|Proteomes:UP000239181}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342 {ECO:0000313|EMBL:PRD14267.1,
RC   ECO:0000313|Proteomes:UP000239181};
RA   Siqueira K.A., Liotti R.G., Mendes T.A., Soares M.A.;
RT   "Draft genome of two endophytic bacteria isolated from 'guarana' Paullinia
RT   cupana (Mart.) Ducke.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:PRD14267.1}.
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DR   EMBL; PDET01000012; PRD14267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S9I909; -.
DR   OrthoDB; 9770795at2; -.
DR   Proteomes; UP000239181; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00088; HPT; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR019247; Histidine_kinase_BarA_N.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF09984; sCache_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PRD14267.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          200..252
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          299..520
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          666..782
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          811..909
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          251..289
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         715
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         850
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   909 AA;  101839 MW;  4A757568A6FD627A CRC64;
     MTKYSLRARM MILILAPTLM IGLLLSTFFV VNRYNELQSQ LTDAGINIIE PLAVSSEYGM
     TFRSRESVRQ LVSLLHRRHS DIVRAISVFD DHNRLFVTSN YLQNPDLLRM PDNTPLTARY
     LKERHGNSVI LRTPILSESY YPDESPGWDA KPTGNPLGYV AIELDLQSVR LQQYKEVFIS
     TLLVLLCLCI AMLFAYRLMR DVTGPIRNMV STVDRIRRGQ LDSRMEGYML GELDVLKNGI
     NSMAMSLTAY HEEMQQNIDQ ATSDLRETLE QMEIQNVELD LAKKRAQEAA RIKSEFLANM
     SHELRTPLNG VIGFTRQTLK TTLNSTQRDY LNTIERSANN LLSIINDVLD FSKLEAGKLV
     LETIPFPLRA TLDEVVVLLA QSAHEKGLEL TLNIQSDVPD NAIGDPLRMQ QIIVNLLGNA
     IKFTERGNID IRVEKRALSN NRMELEVQIH DTGIGISEKQ QSQLFQAFRQ ADASISRRHG
     GTGLGLVITQ KLVNEMGGEI SFHSRLNHGS TFWFHVNLAL NPNAASDPHM LDCLTGQHLA
     YVESNTAAAQ AMLDMLSATP MKVSYSPSLA GLQEAHYDVL LLGLPIDVHN TQEITGEQLS
     PMLQRANSLI LALPFQMQIY AEQLKARGVT ACLIKPLSMA RLLPILVDHH ARDIPPQSGS
     SRLSIRVMAV DDNPANLKLI GALLEELVEH IVLCDSGESA IQQARQQNLD IILMDIQMPD
     IDGIRASEVI RELPQHHNTP IVAVTAHALE GEREKLAKAG MNDYLAKPID EQKLSHLLAR
     YLPARKETLL LPQSGPVSLD WALALRQAAN KPDLARDLLQ MLVDFLPEVR TLVEQFMETN
     NPAGLRDIIH KLHGSASYSG VPHMKKLCQE LEQSLMKHED IAAIEPELLE LLDEMDNVAQ
     LAREQLKIS
//
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