ID A0A2C1K3F1_9BACI Unreviewed; 1190 AA.
AC A0A2C1K3F1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=COD11_20190 {ECO:0000313|EMBL:PGT80756.1};
OS Bacillus sp. AFS040349.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT80756.1, ECO:0000313|Proteomes:UP000222674};
RN [1] {ECO:0000313|EMBL:PGT80756.1, ECO:0000313|Proteomes:UP000222674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS040349 {ECO:0000313|EMBL:PGT80756.1,
RC ECO:0000313|Proteomes:UP000222674};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGT80756.1}.
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DR EMBL; NUMC01000104; PGT80756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1K3F1; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000222674; Unassembled WGS sequence.
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:UniProtKB-UniRule.
DR CDD; cd16434; CheB-CheR_fusion; 1.
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; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR035909; CheB_C.
DR InterPro; IPR022642; CheR_C.
DR InterPro; IPR000780; CheR_MeTrfase.
DR InterPro; IPR022641; CheR_N.
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; 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:SF25; CHEMOTAXIS PROTEIN METHYLTRANSFERASE; 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; 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; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
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); 2.
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 Chemotaxis {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00050};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:PGT80756.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000222674};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 17..206
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 203..479
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 841..900
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 914..966
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 979..1185
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 662..734
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 29
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1190 AA; 136268 MW; 922D6FA80C2CB70D CRC64;
MSNASNGQLE KEHEKGDLDT PYVVGIGASA GGLEAIEQFF QNMKSNIDAA FVVVQHLSSK
YKSFMPELLV KYTNMKVLVA KQGLQVNPKT VYLCPPNHYI TINNQGRIHL ETYHESQVVN
YPIDAFLTSI SLYAKKKAIG VILSGKGTDG TKGLNDIHER NGLCIVQNET AKYMDMPESA
IKSGVGDYII NPSVMPEHIQ NYIETKPVEF KETTLKQVLM MIHKKSGIDF TMYKKNTVIR
RIERRMSLLE ESFLNLEDYK NYLLANPREI RYLQEDLLIG VTHFFRDTDA FYYMQQTLIP
SMVDENLQRG RNKMRIWVAG CSSGQEAYSL AILFNEELEK RESDMDLQVF ATDIDRDAVK
FASQGCYSEQ IVSMIPKHLL IKYFDKQGSD YQVKREIRQK IVFAPHNMTK DSPFVNLDMI
SCRNVMIYFQ TELQQRVLSL FHFALKEKGY LFLGPSETIG KLSNLFSSVN SKWKVFSNQV
SDNQHFSQAL LAPKEVSGDS ERRGTEHLRD TNRFQHPDEL YYSLMDDLLP PCIVINEHNE
VILSSGNAGE YLNLPKGKVN YNIFNMVPTN LSVAIGTAIK KVREELREIK YKNLLINKNE
SKQVKLVVKP LENVRKGYVA LFIKDHMPDS TTIIKADSMT FDQDSAYNQR IFDLEQELYY
TKQSLQTTIE ELETSNEELQ STNEELIAAN EELQSTNEEM QSVNEELITV NSQYEKKIIE
LTDLNNDMDN LLINTNIATI FLDKKLNIKL YTPEVMKLFH VIDRDIGRPI FHISHRLECD
TLMDEIQDVL MTTNSIIKDL PAKDGKWYSV KIMPYRTSDN IVDGIVMTFI DITKIKKVNR
ELQLSMQAIE LSPANTVFTD FQGKIEYANS KFAEQLGLEV KDLIGRKLKD IYAEYYIDSD
FDSHWKKVRA GEKWSGEISY TARDGKQYWE NLALIPVEND DHDVVQILRV GEDVTNRKSS
EQMLIKSEML SAIGQLAAGI AHEIRNPLTS LRGFLQLMIQ TNTYRKEYAE VMMTEFIRLE
EIINEFLVLS RPKTAAFQDV NINKIIQDVS KIWGTQAILN DVTIETYNDP FIFTIQGIEN
ELKQVFINIV KNGIESMEGR PGNLKIETRK LDSGEVLIRF EDKGKGIPKE QLEKMGQPFY
TTKEKGTGLG LMVSFKIIES HNGKIVFSSE LDKGTTVEIT LPLSNSVEAV
//
