ID A0A109LRK2_9SPHN Unreviewed; 657 AA.
AC A0A109LRK2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASS64_14615 {ECO:0000313|EMBL:KWV92481.1};
OS Erythrobacter sp. AP23.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=499656 {ECO:0000313|EMBL:KWV92481.1, ECO:0000313|Proteomes:UP000058666};
RN [1] {ECO:0000313|EMBL:KWV92481.1, ECO:0000313|Proteomes:UP000058666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP23 {ECO:0000313|EMBL:KWV92481.1,
RC ECO:0000313|Proteomes:UP000058666};
RA Lin W., Zheng Q.;
RT "Draft genome sequence of Erythrobacter sp. AP23.";
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 -!- 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:KWV92481.1}.
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DR EMBL; LNBY01000020; KWV92481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A109LRK2; -.
DR STRING; 499656.ASS64_14615; -.
DR OrthoDB; 9801651at2; -.
DR Proteomes; UP000058666; 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 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; IPR007891; CHASE3.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF05227; CHASE3; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:KWV92481.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:KWV92481.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 278..350
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 352..404
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 422..639
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 657 AA; 72727 MW; D9D9D8BE16426606 CRC64;
MRHANRTKRS AGRIWANRPL AYKGVLLVGI PLAVLFGALG SLYLASSAEA RAEDDVRRAF
EIQRDTYQVH ALLSEAAAAV RSYVLTRDRS LLAPYDKARQ ELPPIMESLD QAIEDAGVRS
EFEALSALVE DKSASQARLV GLATANQPGP EGALIRAELA ASSAVLDELG DRVDSMQRAE
AELLERRRAT VDNVRERYFA LTAISALFGL LGSLAAVYLF STGIVRRVRI LENNAGLLAR
GERLLELPEE ADEIGRLGEK LARASDLLRA REKDLSESEE RFRLVIDRVR DYGIFALEPD
GTVATWNLGA ERIKGWRAEE ILGRHFSTFY PQETRDRLPA IMLQKARKEG AAEDEGWRMR
KDGSRFWANV VITALRDADG TLRGFAKVTR DMSERRRTEE ALLAAREEAI AADQAKTAFL
SRTSHELRTP MNAILGFGQL LEMEEDSFAD HHRSAVQQIM KAGRHLLSVI NDLLDISSIE
AGAEDLQLEP VNLNDLLREA HSMGAPLVRA ADLQFQIEAA DNRIEMMVDK RRTLQVCLNL
IANAAKYNLN GEFVRLSGRM DKDLVRIEIA DDGPGIATKD IPRLFTAFDR LGQNERSTVE
GTGLGLALSK SLVGSMGGTI GYDRERFGSI FWFALPAMGN AQEASESHDK GTLTEDD
//
