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Database: UniProt
Entry: A1K587_AZOSB
LinkDB: A1K587_AZOSB
Original site: A1K587_AZOSB 
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
//
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