ID D3NZI0_AZOS1 Unreviewed; 598 AA.
AC D3NZI0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=AZL_a02780 {ECO:0000313|EMBL:BAI73809.1};
OS Azospirillum sp. (strain B510).
OG Plasmid pAB510a {ECO:0000313|EMBL:BAI73809.1,
OG ECO:0000313|Proteomes:UP000002040}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=137722 {ECO:0000313|EMBL:BAI73809.1, ECO:0000313|Proteomes:UP000002040};
RN [1] {ECO:0000313|EMBL:BAI73809.1, ECO:0000313|Proteomes:UP000002040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B510 {ECO:0000313|EMBL:BAI73809.1,
RC ECO:0000313|Proteomes:UP000002040};
RC PLASMID=pAB510a {ECO:0000313|EMBL:BAI73809.1};
RX PubMed=20047946; DOI=10.1093/dnares/dsp026;
RA Kaneko T., Minamisawa K., Isawa T., Nakatsukasa H., Mitsui H.,
RA Kawaharada Y., Nakamura Y., Watanabe A., Kawashima K., Ono A., Shimizu Y.,
RA Takahashi C., Minami C., Fujishiro T., Kohara M., Katoh M., Nakazaki N.,
RA Nakayama S., Yamada M., Tabata S., Sato S.;
RT "Complete genomic structure of the cultivated rice endophyte Azospirillum
RT sp. B510.";
RL DNA Res. 17:37-50(2010).
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; AP010947; BAI73809.1; -; Genomic_DNA.
DR RefSeq; WP_012975705.1; NC_013855.1.
DR AlphaFoldDB; D3NZI0; -.
DR KEGG; azl:AZL_a02780; -.
DR HOGENOM; CLU_000445_133_5_5; -.
DR OrthoDB; 7325042at2; -.
DR Proteomes; UP000002040; Plasmid pAB510a.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAI73809.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:BAI73809.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002040};
KW Transferase {ECO:0000313|EMBL:BAI73809.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 55..126
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 130..182
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 183..243
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 254..304
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 338..584
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 295..329
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 598 AA; 65756 MW; 62C1C782CF125361 CRC64;
MAAEPVMVAL AVGAVGGLLG MLLGLHAGRR SARRPLPTAT SAVTVSGIPV HDPEIGQRLE
MALEATGAAV WDADLVAGTC WWSDTFPRML GYRSRPPMPP DFWERRLHPE DRDRVLAHIA
SHLAGETSAY AYSYRLRHEG GGWVWIAAKG RAFRDESGRA VRYAGIMTDI TESRRQEERL
RASEERLLKI MEAAPIAVNV TTRDGRWLFC NAQSVRLMGR DRTELMRTPV AELYDDPADR
EALIARFDRE GAFRNVEIRF RRPDGSIVWA LSSWNSIELD GESALLTWLY DITDRKAVES
AMIQAREEAE QALADLREAQ ESLIQAETMA SLGQLVAGVA HEINTPIGIG LTAASHIGEQ
AQILRERFTG NALRRSEFLE FLDGLSESSR LLMANIDRAA SLVQSFKQVA VDQSSGDRRV
FELGSYIREL LFSLRPRLKR TNLTVAVECD DDLTMDSFPG ALGQVLTNLV INAVIHAYGD
GDRLSDRGGD RLAERPDGTI RIIAQPDGRD KVRIDFVDDG VGIAPEHLSK VFDPFFTTKR
GQGGSGLGLH IVFNTVTGPL GGTVSVQSWP GQGTRFTMLL PREAPALQPA AVQEPALG
//
