ID A0A0C4WN35_9GAMM Unreviewed; 915 AA.
AC A0A0C4WN35;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Achr_13480 {ECO:0000313|EMBL:AJE20820.1};
OS Azotobacter chroococcum NCIMB 8003.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=1328314 {ECO:0000313|EMBL:AJE20820.1, ECO:0000313|Proteomes:UP000068210};
RN [1] {ECO:0000313|EMBL:AJE20820.1, ECO:0000313|Proteomes:UP000068210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 8003 {ECO:0000313|EMBL:AJE20820.1,
RC ECO:0000313|Proteomes:UP000068210};
RX PubMed=26061173;
RA Robson R.L., Jones R., Robson R.M., Schwartz A., Richardson T.H.;
RT "Azotobacter Genomes: The Genome of Azotobacter chroococcum NCIMB 8003
RT (ATCC 4412).";
RL PLoS ONE 10:E0127997-E0127997(2015).
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; CP010415; AJE20820.1; -; Genomic_DNA.
DR RefSeq; WP_039802979.1; NZ_CP010415.1.
DR AlphaFoldDB; A0A0C4WN35; -.
DR STRING; 1328314.Achr_13480; -.
DR KEGG; acx:Achr_13480; -.
DR HOGENOM; CLU_000445_105_0_6; -.
DR Proteomes; UP000068210; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000068210};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..915
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002173277"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 413..634
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 786..907
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 837
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 915 AA; 101691 MW; 64EB32C19521B539 CRC64;
MVRIVWMLLL LLIGASAWAI QPAVLADQEV RLSLGPHTRY LEDRDASLDA AQVLALPDTA
FRPVEGDRAS LGRSRSVWWF RIDLQNTRTQ PLSGFLEVNY PLLNDVRLSL LSPDGQLQQQ
ESGDARASQR RPVPVRNLWF PLELPPGSST LLVRVKSSSA ITVPLYFSTS GASVVVQERQ
EGLNGVFYGV LLALFCYQLL LFLFLREPSQ GWYLLYSLNA ILLPFSFDGF LFHWSPVLQQ
VAVYLLTFTF WLSATQFTRH FLNIPQYFPL LDRALRLWML VLAAALLAAP LIGLPAWGVL
ATLATLIGSL LLPACGAHVW RKRLRAGTYQ LAAWALLLAL LAGLACTELG LGLGLLGEQG
TTLAKLGLAV NLLVLAVGLA DRFQQLRKEG LYSHQAAEEA LLQNQAKSRF LAKMSHEIRT
PLNGVLGMLQ LLKETRLDHS QRFYVDTIAS SGSTLMAVIN DILDYARIES GKLSLEHIEF
DLEEMLSDTL NLFTAQAMEK RLRLHMSLDE GVPRHIQGDP TRLKQVLTNL LSNALKFTSE
GQVRLDVSRR RKSDGSERLY FGVSDSGIGI RQEAQARLFE SFSQGDSSTT RRYGGSGLGL
AISKELVEMM GGHIEAQSTP GLGSRFTFNI PLQRCGEARD ELFQLLVGRT ALLASLDGFA
LDAIGRLLGR WGMHTERCRI PEKLPEQLTG FDEPPLLLLI APWPGSVEYW LDALYPHLAP
GQRLLLVCPP EQCRQLPASR SSLHMLGLPQ PVGVAALRKK LVELLMEPTH SLVPIEDPAG
DSQVPCILIA EDNPVNQLVV QELLKKRGYH VRLAGNGAEA VAEYHRSPGA VQMILMDCEM
PEMDGFEATL QIRLLERLRK WPAVPIIALT AHTLDEHREY GLEVGMNDFL GKPVDKQLLH
ATVERYLSIR TLVDN
//
