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Database: UniProt
Entry: A1K864_AZOSB
LinkDB: A1K864_AZOSB
Original site: A1K864_AZOSB 
ID   A1K864_AZOSB            Unreviewed;      1012 AA.
AC   A1K864;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   Name=barA {ECO:0000313|EMBL:CAL95019.1};
GN   OrderedLocusNames=azo2402 {ECO:0000313|EMBL:CAL95019.1};
OS   Azoarcus sp. (strain BH72).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Azoarcus.
OX   NCBI_TaxID=418699 {ECO:0000313|EMBL:CAL95019.1, ECO:0000313|Proteomes:UP000002588};
RN   [1] {ECO:0000313|EMBL:CAL95019.1, ECO:0000313|Proteomes:UP000002588}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BH72 {ECO:0000313|EMBL:CAL95019.1,
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; CAL95019.1; -; Genomic_DNA.
DR   RefSeq; WP_011766133.1; NC_008702.1.
DR   AlphaFoldDB; A1K864; -.
DR   STRING; 62928.azo2402; -.
DR   KEGG; azo:azo2402; -.
DR   eggNOG; COG0642; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_104_15_4; -.
DR   OMA; KWIQEYQ; -.
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   CDD; cd06225; HAMP; 1.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.20.120.160; HPT domain; 1.
DR   InterPro; IPR033417; CHASE8.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF17152; CHASE8; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00073; HPT; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002588};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAL95019.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          191..244
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          284..505
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          524..645
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          673..787
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          828..929
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   MOD_RES         576
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         722
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         867
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1012 AA;  109109 MW;  FD4A57B79A634CA3 CRC64;
     MKRSARLSDL LHPETIRGKL MVLSVAGLLI GVVLVFALIV YQQQRLIRNE WADSLNAQAR
     LIATNSEAAL AFQDRSEAAR LLAAVQSNPF ILRARLLVGP DGAVFAQYDR GDADPIPDMP
     DAAGDGGAHF AEGWLIVQSR VRTGDGSDAR VELVASLESM RQTEWNLALE TGTMLLLALV
     LSLWLAGRMA HRLSAPVERI SALLQRMSSN AALDERLQVQ GNDEIARLAH GLNTLIDTLQ
     ARDRELNDYR QHLEELVEQR TRQLSIATAE AQQASRAKSD FLARMSHEIR TPMNAVIGLT
     HLALRTELSP QQRDYLRKIR GSSQALLGII NDILDFSKIE AGKLRLEQIP FTLHDVIDNL
     SNIVTVKAAE KGLDVLLAID PAIPDRMRGD PLRLSQILIN LGTNAVKFTE RGEVVVDCRL
     IDKTEDCVRV RFSVTDTGIG ISAAQRGLLF QSFHQADGSI TRRFGGTGLG LAISKQLIEI
     MEGSLEVASE PGEGSTFSFV IPFGTVAGAR ERHYLAPEEL RHKPILVVDD NPTARAMLRT
     MIEHFHFVAD TAASGEEAIL KIREAGEQGY AVVLMDRDMP GLDGIEAARR IKLDLSLPTP
     PRILLMASYT KDHALQEAGH GAGLDGILTK PVGPSLLFNS LLKVLGHAHR VEPEEPLFAD
     QPTQGLAGIR GARVLLVEDN PINQQVATEF LRQAGLQVDL AGDGYEGVDR AVATAYDLIL
     MDVQMPGMDG LEATRRIRAR DSHTPIVAMT AHALDTDRER SRAAGMNGHL TKPIDPAELE
     TTLVRWIPPG VRALPAGTLP AAADTTTEEL PVIDALDGAQ GLKRVGGSAR LYLDLLRDFL
     KGHASDAERV EALVEGGDWA TAGRVLHTFK GVAAALGGTE LAALAVRVED AVREQNRGAA
     VEALPPFTRA LGNLCGALAE HFARHPGGAP AASASVGATE GPDLREGLEQ AAELLRAGNS
     RAERVVASIA PAAHAQGHGG EVDAILAAIE DVEFDAALAR VNALLARFER NG
//
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