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Database: UniProt
Entry: Q1H3K0_METFK
LinkDB: Q1H3K0_METFK
Original site: Q1H3K0_METFK 
ID   Q1H3K0_METFK            Unreviewed;       703 AA.
AC   Q1H3K0;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Mfla_0667 {ECO:0000313|EMBL:ABE48937.1};
OS   Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylobacillus.
OX   NCBI_TaxID=265072 {ECO:0000313|EMBL:ABE48937.1, ECO:0000313|Proteomes:UP000002440};
RN   [1] {ECO:0000313|EMBL:ABE48937.1, ECO:0000313|Proteomes:UP000002440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT / ATCC 51484 / DSM 6875 {ECO:0000313|Proteomes:UP000002440};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT   "Complete sequence of Methylobacillus flagellatus KT.";
RL   Submitted (MAR-2006) 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; CP000284; ABE48937.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1H3K0; -.
DR   STRING; 265072.Mfla_0667; -.
DR   KEGG; mfa:Mfla_0667; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_15_4; -.
DR   Proteomes; UP000002440; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABE48937.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002440};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABE48937.1}.
FT   DOMAIN          343..562
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          580..698
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         631
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   703 AA;  78044 MW;  45FC7D0F76EAA976 CRC64;
     MSVNLDSYPA PPRCREESLP LKAPTMHDAT PSSMGEDEYQ FLLKLSSTIR PLVNTEEIKR
     CVCKMLCEAM SAERAIYSEI SAVGDAMINV SYQTPGIAEI HGKFELDQFG KDLMGRLHMG
     ETLIMQNIQQ EASLNAEERQ AYASVGVQSY IAVPLIKQST LMAVLSVNAT TPRRWSRRDA
     LLLQKVAERT WETVERARAE HALCLTEMRS QQIFDSIDQG MCIIRMVYDR DGKPIDYIFL
     HANAAFASQT GLANVIGKGM RELAPHHEQF WFDTYARIDR TSIPERFEHK AEALKRFYEV
     YGFRIDDPEE HTVCVLFKDI SSRIAAEQAL LKANKAKDDF LAVVSHELRN PLNLILLNAE
     LLARIPEAQT QPIIQRTAET LSRTVKNLAI VVDDLLDLSR INTGKLALQC HSLHFEPLVR
     RLITSFQDEA QHNGIALSHA LQPNLLIHAD AARIEQVIWN LLSNALKFTP SGGAIHVSLS
     SRDDWAILEV SDTGQGIAAE VLPHVFDMFV QEDSSSSRIK GGLGIGLALV KQIVELHQGK
     VEACSRGKGT GANFRVFLPL SRTVPAEASQ DPSTLNHSVR LLLIEDNQDS ADLLSHLLTL
     EGYQVDVALG GKSGLEMIDT AEYSYDLILS DIDMPDLDGF QLARRLRANE KTVTTPLIAV
     TGINLQGNCE KLYSAGFDDV VSKPVSVAAI HAALRKQLHR HSG
//
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