ID J2H0S2_9CAUL Unreviewed; 456 AA.
AC J2H0S2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=PMI01_01010 {ECO:0000313|EMBL:EJL36385.1};
OS Caulobacter sp. AP07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL36385.1, ECO:0000313|Proteomes:UP000007300};
RN [1] {ECO:0000313|EMBL:EJL36385.1, ECO:0000313|Proteomes:UP000007300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP07 {ECO:0000313|EMBL:EJL36385.1,
RC ECO:0000313|Proteomes:UP000007300};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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 -!- 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:EJL36385.1}.
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DR EMBL; AKKF01000066; EJL36385.1; -; Genomic_DNA.
DR RefSeq; WP_007663947.1; NZ_AKKF01000066.1.
DR AlphaFoldDB; J2H0S2; -.
DR PATRIC; fig|1144304.3.peg.960; -.
DR Proteomes; UP000007300; 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; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR013727; 2CSK_N.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR45436:SF15; SENSOR HISTIDINE KINASE CRDS; 1.
DR PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR Pfam; PF08521; 2CSK_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJL36385.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW 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 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..238
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 246..456
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 456 AA; 49479 MW; 0A7776CD85B5BCBA CRC64;
MRLRSLTARL LLALVVPLIV SALIVGVGGA WVTQRVVDYS SDRLLAGSVR AIAESITVEN
DKVWVDLPPW SLGLLDSPQR DSVYYNVRQG GRVLTGYRDL PDFDRAAIAS RKPTFRTVRY
KGVMVRQAAE ARHVPGVAAP VIVSVAQTLD SRLAARNTLL ASLGLVEAVL VALVALLIWP
AARWGLRPLD ALRRELAQRS VSTDLDFTPL RLDHVPGELT PVVGAFNGLL AQLDQAVEGM
RRFTADASHQ IRTPLAVMKV HLGVMGRRRD RSQEDQDSLA DVLDGVNRLQ RLLEQLLALA
RADVADQSAL EHADLALTVR RDLARLQADL DRKSVSYRGP EQDVWVAMSA TLIEQILENL
VDNAVRYGGE RIVVTVSAEA DLAVVEVADD GPAVPPEAAE RLFERFHRAP DAEAPGSGLG
LSIVRALAER SGGAAVIVVP PASKGFTVRV TLPRAE
//
