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Database: UniProt
Entry: L0KF06_MESAW
LinkDB: L0KF06_MESAW
Original site: L0KF06_MESAW 
ID   L0KF06_MESAW            Unreviewed;      1516 AA.
AC   L0KF06;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Mesau_01449 {ECO:0000313|EMBL:AGB43917.1};
OS   Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB43917.1, ECO:0000313|Proteomes:UP000010998};
RN   [1] {ECO:0000313|Proteomes:UP000010998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC   {ECO:0000313|Proteomes:UP000010998};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA   O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium australicum WSM2073.";
RL   Submitted (FEB-2012) 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};
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DR   EMBL; CP003358; AGB43917.1; -; Genomic_DNA.
DR   STRING; 754035.Mesau_01449; -.
DR   KEGG; mam:Mesau_01449; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_003919_0_0_5; -.
DR   Proteomes; UP000010998; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 6.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 4.
DR   Pfam; PF12860; PAS_7; 3.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 7.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010998}.
FT   DOMAIN          439..509
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          703..773
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          776..827
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          831..901
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          903..954
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          972..1192
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1210..1331
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1387..1505
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1336..1379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1264
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1436
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1516 AA;  166816 MW;  0AC663DA87A14298 CRC64;
     MAESDEAIGV RGKRKPGKAA APGGDGPSGV DMDCADALRQ LVEAGSDWIW ETDAELRFSW
     LSQDYQAATG IDPAMVLGRF RFDFLNQVLK GNRGAAAHLE DLQAHRPFRD FVYELKGGRP
     DCSWVLTSGF PRFDSEGKFV GYRGLGRNVT ALASAFEAMQ PAAGGDAVQH LADLERTMDA
     MHMGVVLLDA RLDTLIVNKA YRDLSRIPDG AVTVGAPFSL LMELNRRNGI YGDIDEEQWQ
     RYLATRIEEI KAGTVAPREF AHTDGRTMMF SVTALSGGKR LLTYYEVTEV KRRDAEIENA
     NAKIAETFAN LRTMVDQMPI GVLVLDADMR AEVINRAFYD FWQIDARRAE TGCSFLDLME
     ASRDIDPYGS DDATWHRHVA EREAEIRAGT AGARQFPRND GRTLISSMAP LAGGKRFISY
     VDVTDMKDRE AELAEALEKA RLAEAVINGV KDPIFVKDDN LRFVFVNEAF AALFKQAPQA
     MLGRPGSDFL GPDEVALFES SEREVLAGGQ QYEVEESFEA GGGIRSRIVR KNRVRMASGR
     DYVAGFLFDI SDMKRRETEA EDARKHLASV LESLPAGVII YDRDDKFVFA NHRLQDTLPA
     LKPFWQPGRT FREALEFGHS VGYFRSSGDP GIDSLYEGDS ERWLDGILAR YRLPNSSYER
     LNADGRWYQV YDMRTGDGTF IGVRVDITDL KSREAALHDS MRQIDLFRHV MDELPVAAFI
     KAQDLSIEFV NKAWCALTGL AKDDVIGRAD RQLFNGEEAE GFSQDDTDVV TNGNVREVEE
     PVTHRDGTVR QLMTRKSRLV ATDGSVHLVG SSTDITDVKA REQALEESMR ENEVFRSLID
     NVPVSIYAKR SDLRQFYVNK GWCDLTGFSK QEAIGKTDVE IFGPDGEAFV ASDLAVLRTG
     ETQEIEETVR LPDGSVRHQF ARKGAMIASD GSLYLIGSTT DITELKQREA ELSEARRRAV
     LADRAKSEFL ANMSHEIRTP MNGVLGMAEL LAKSNLDPKQ KTFTDIIVKS GNALLTIIND
     ILDFSKIDAG QLVLDPAPFN LAEAIEDVAT LVSTRAKEKD LELIVRIEPR LESLFIGDVG
     RIRQIVTNLL GNAVKFTDEG HVLVDVTGER VPTGTRLTIS VTDTGIGIPE EKLKLVFEKF
     SQVDTSSTRR HEGTGLGLAI TSRLVDLMGG DIGVESAEGK GSTFWFTVTL PGAGQQSGQR
     ITPVDVTGAR VLIVDDNAVN RAILTEQMTS WTFDSCAAES GAEGLKVLIA AAAYGVAVDC
     VVLDYQMPEM SGAEMARIVR NTEGLADTPI IMLTSVDQSL ANTSYRDLGI DAQLIKPARS
     SVLLETLVAT IQRHRHATSG HAVQPLTGEA PEASRPPPLA PSEQRAQLQP PQVRPRLPAT
     AGGHRLDILV AEDNEVNQMV FTQILGETGY GFEIVGNGRK ALDAFGTLNP CMILMDVSMP
     EMSGLEATAA IRLLEQETGT HVPIVGVTAH ALKGDRERCL EAGMDDYLPK PISPRALLEK
     VERWVGAGRQ VHRNAG
//
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