ID A0A0M5JL50_9BACI Unreviewed; 1176 AA.
AC A0A0M5JL50;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 18-JUN-2025, entry version 43.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AM592_02130 {ECO:0000313|EMBL:ALC80514.1};
OS Bacillus gobiensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC80514.1, ECO:0000313|Proteomes:UP000067625};
RN [1] {ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALC80514.1, ECO:0000313|Proteomes:UP000067625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC80514.1,
RC ECO:0000313|Proteomes:UP000067625};
RX PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00050}.
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DR EMBL; CP012600; ALC80514.1; -; Genomic_DNA.
DR RefSeq; WP_053602248.1; NZ_CP012600.1.
DR AlphaFoldDB; A0A0M5JL50; -.
DR STRING; 1441095.AM592_02130; -.
DR PATRIC; fig|1441095.3.peg.460; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000067625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0008984; F:protein-glutamate methylesterase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.40.50.180; Methylesterase CheB, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050903; Bact_Chemotaxis_MeTrfase.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P_dom.
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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR000673; Sig_transdc_resp-reg_Me-estase.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR24422; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 1.
DR PANTHER; PTHR24422:SF10; CHEMOTAXIS PROTEIN METHYLTRANSFERASE 2; 1.
DR Pfam; PF01339; CheB_methylest; 1.
DR Pfam; PF01739; CheR; 1.
DR Pfam; PF03705; CheR_N; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13596; PAS_10; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00996; CHERMTFRASE.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00138; MeTrc; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47757; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF52738; Methylesterase CheB, C-terminal domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50122; CHEB; 1.
DR PROSITE; PS50123; CHER; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000067625};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 15..173
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 195..478
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 842..886
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 907..959
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 972..1176
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 644..696
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 772..799
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1176 AA; 135018 MW; 00B20AD000A18D4D CRC64;
MHEELLNFMP ENQKLTPSSI IIGIGVSVER LDALFDYFKD VKPLHSLSYI VVQTPSVKHK
GFTASLMEKY LSLNVEMAEQ GSAIMANTVY LSPPEHYVEI LENKTIKLTP YTIIENNHFP
INVLLKSLAK TQKEKAIAIV LPGKERDGFE GLKIVHQYNG FSTVQDAAGA SMYSFANVFA
APENIAGYIN QLHESMDDYD SFSEGAIDQI LYKIQNQNGV DFSMYKKKSI LRRIERRMKL
LGHPLETLDE YMIFILDHPE ELQRLHDDLL NGITHFFRDE EFFYQLRKTY IPKIIENNIK
KDKQTCRIWI AGCSTGEEAY SYAILFSEEL EKRKLDIDLQ IFATDINRRS IQKASKGSYT
ENEVSSIPSD WLKKYFDKTG QRYSVKKILR NHIIFAPHNL IRDTPFVNLD FISCRNVMIY
FQRKLQEKAL SLFHFSLCDG GLLVLGPSET IGNQSEVYQP VDWKWKIFKN SFYDQKAKRN
RFHLNALEAG KALANTFENI DERKNLQLDE LYLSLIDQFL NPFLIINDQE EIIASSPNAS
QFLKTPAGSP SNSIYSRLSA DLSVPISSAL KKIKDHKSEI RRNHIKVTIN GAPVFVEITV
RRFKFNVRHY PLYVLFIHKE LEGIKTNKKE FLMLDQEIYP NHCIQKLEML INETNSKLQT
TIEELEISND ELRSTNEKLI ADNEELQTSN EELQVVNEDL MTVNGNFEKK IEELSSTAGE
MEKMLINSNI ATVFLDNEYN IKLFTSEAAN VFHLIDRDVG RPIYHIASRL NYREFLDDAK
KALNEMKTIQ KEVEADNKDI YIVKMIPNLS NGTKADGLVI LLVNITDLKA TNKALQVGSH
RIEHSNSSIV VASPSGRIKY VNINFCSILG KEQFEIIGQN IFDIYQNSFK VHEFKDHWDH
VLKHKSWTGE EYSQGRNGTD LWEKVSFITL EDNEGNIQQI MRVAEDITHQ KNSEKMLMKS
EMLSAIGQLA AGIAHEIRNP LTSLKGFLQL MIQSNTYHKE YAEVMQSEFI RLESIINEFL
FLSKTKSSKF ETICVNDIIE DVYLILEAQA MLKGVRITKA LCQDVNEVRA VPSELKQVFL
NILKNAIEAM EELEGEILIQ SKGEEDRVLI MIKDQGKGIS KDFLDKLGEP FYTTKEKGTG
LGLMVTMRII ESHKGEIIFE SEEDQGTTVK IYLPCL
//
