ID A1K587_AZOSB Unreviewed; 904 AA.
AC A1K587;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=azo1375 {ECO:0000313|EMBL:CAL93992.1};
OS Azoarcus sp. (strain BH72).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Azoarcus.
OX NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL93992.1, ECO:0000313|Proteomes:UP000002588};
RN [1] {ECO:0000313|EMBL:CAL93992.1, ECO:0000313|Proteomes:UP000002588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH72 {ECO:0000313|EMBL:CAL93992.1,
RC ECO:0000313|Proteomes:UP000002588};
RX PubMed=17057704; DOI=10.1038/nbt1243;
RA Krause A., Ramakumar A., Bartels D., Battistoni F., Bekel T., Boch J.,
RA Boehm M., Friedrich F., Hurek T., Krause L., Linke B., McHardy A.C.,
RA Sarkar A., Schneiker S., Syed A.A., Thauer R., Vorhoelter F.-J.,
RA Weidner S., Puehler A., Reinhold-Hurek B., Kaiser O., Goesmann A.;
RT "Complete genome of the mutualistic, N2-fixing grass endophyte Azoarcus sp.
RT strain BH72.";
RL Nat. Biotechnol. 24:1385-1391(2006).
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; AM406670; CAL93992.1; -; Genomic_DNA.
DR RefSeq; WP_011765108.1; NZ_CP016210.1.
DR AlphaFoldDB; A1K587; -.
DR STRING; 62928.azo1375; -.
DR KEGG; aoa:dqs_1497; -.
DR KEGG; azo:azo1375; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3452; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_011685_0_0_4; -.
DR OMA; QTGWMTS; -.
DR OrthoDB; 1931120at2; -.
DR Proteomes; UP000002588; Chromosome.
DR GO; GO:0016020; C:membrane; 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; 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; 3.
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; 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; 3.
DR PANTHER; PTHR43065:SF47; COMPONENT HISTIDINE KINASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CAL93992.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002588};
KW Transferase {ECO:0000313|EMBL:CAL93992.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 287..357
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 407..479
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 483..535
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 536..574
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 679..895
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 904 AA; 101266 MW; 7CBC252F0819A84A CRC64;
MPHSEKSTAL QAPLRWYWTA PYAAVVVFAL SMLALVWLLQ TREEESQRSA VARDVQWAEQ
TMRLHMQGTE EFLAQLARDL ANETLDPDAF QVRANQHIAN SGELVNITWV GADEIVRWSA
PFDTTDWLAG DALTPPQALA FNRARDFGRA VYGEAYRNPR GGMVLEVYVP VRHGRGFRGA
VVGVYSIEGM VRYLVPGWFA EKYRLALENG RGDTLAVNSA VRDTDETLSF QIPLDPPGNG
LTLRATAFKA HGAVPQALPA VLIVGLSVIV LWSLWMLRGH VLRRVQVEKE RDRLFNLSLD
MLCVVGFDGA FRRCNPAFEH ILGYAPETLP GLPLLEIVHR DDIASTLEQM RRLAGGEPVK
FENRCRCADG NYKWLMWSIN PVREEKLVYA VAHDITGRKA AEEALRAESA FRKAMEESVL
TGLRAIDLSG RIIYVNSAFC RMVGFSEKEL VGASEPFPYW PSEDLEFCRR NLELTLAGRA
PPSGFEMRIR RKNGERLDAR FYLSPLIDLE GRQTGWMASV TDITEPKRVR AALEATHERF
EAVLDGLDAA VFVADARTDE ILFANRAFKT IHGFDTVGRT VRGVAVPQPE RGDYRVDPRG
LTVGDLPREL FDGELQHPLS GRWYHVREHA TRWVDGRVVR MGIATDITDR KQTAEVSRQQ
EERLQRTARL ITMGEMASTL AHELNQPLSA IANYCAGCVT RMQGDNWKQE DILGAMQKAS
FQAERAGKII RRIREFVKKS EPRRSAVQIG EVLDDALGFA DIDARRVGIR IVAAVDPDLP
AVYADRIMIE QVVLNLVRNG LDAMADTLPE ERELVVRARA FGPHAVEVAV IDRGHGIGEE
DRQRLFTPFY TTKAEGMGMG LNICRSIIEF HDGRLVVDGN PEGGTIFSFT LPTEAASERI
ARRA
//