ID A0A0Q7U920_9CAUL Unreviewed; 747 AA.
AC A0A0Q7U920;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASD21_19685 {ECO:0000313|EMBL:KQZ04031.1};
OS Caulobacter sp. Root1455.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736465 {ECO:0000313|EMBL:KQZ04031.1, ECO:0000313|Proteomes:UP000051447};
RN [1] {ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|Proteomes:UP000051447};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ04031.1, ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|EMBL:KQZ04031.1,
RC ECO:0000313|Proteomes:UP000051447};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:KQZ04031.1}.
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DR EMBL; LMFQ01000005; KQZ04031.1; -; Genomic_DNA.
DR RefSeq; WP_056437395.1; NZ_LMFQ01000005.1.
DR AlphaFoldDB; A0A0Q7U920; -.
DR Proteomes; UP000051447; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
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; IPR017232; NtrY.
DR InterPro; IPR045671; NtrY-like_N.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF19312; NtrY_N; 1.
DR Pfam; PF00989; PAS; 1.
DR PIRSF; PIRSF037532; STHK_NtrY; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KQZ04031.1};
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}.
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 62..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 329..382
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 513..732
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 747 AA; 80628 MW; 0E04615CF7E8707D CRC64;
MASVPSVLEL EGPPTRFSRA WWRELLRSRF TLGGAYGVAI ALTATAVGLA SSPPATGPIG
PATTVILAVL GFNLALILCV AGIVGWRLLD LVDARASDAG ARLHLRFVGL FSVAAVAPAV
IVALFFGVLV NRGVDAWFSE RVRTVVENSA TVARSYVTEQ TEYISQHVGP MAGTLNQAAP
TLVDSPVAFG HYMKEHMEEN GFSAAYVLDR DGRILARAES DTAPPFLAPP PSSFRRTDSG
DITSQRFVEE DLFRALYRLR AFPDAYLYVA RPIDKGILAH LIESEESLIS YREAAKNQDR
IQVIFGLSYI ETALLVLVAA VWVGIAAANS IAAPVSGLVQ AAGRVSAGDL DARVDVEIGP
EEIRALSIAF NMMTTDLQAQ QAALRVASLD AESRRQFIET VLSGVSAGVI GLDADGRITA
LNRRAGDLLA LTDDAVGQPL VELAPELETV IQEISGGKPT AEVEIDVIRG GETRRLRFRG
AGHAVGTLVL TFDDITRLVA AQRNAAWKDV ARRIAHEIKN PLTPIQLSAE RIRRKYRKDI
TSDLDTFDRC TETIIRQVGD IGRMVDEFSS FARMPAPRFA PADLAEMLRQ AVFAQRFVDT
ETEVALEEPG EDVWISCDAR MVGQALTNIL KNAGEAVGAR RQATPEPPGR IVASLVSDDE
HLCIVVEDNG VGLPARDRDR LTEPYVTTRE KGTGLGLAIV KRIMEDHEGE LVLTDALNGT
GARVILKFPT TARLAAANAQ SGVEEMI
//
