ID A0A2W1LKM7_9BACL Unreviewed; 1196 AA.
AC A0A2W1LKM7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Histidine kinase {ECO:0000313|EMBL:PZD95445.1};
GN ORFNames=DNH61_12995 {ECO:0000313|EMBL:PZD95445.1};
OS Paenibacillus sambharensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1803190 {ECO:0000313|EMBL:PZD95445.1, ECO:0000313|Proteomes:UP000249522};
RN [1] {ECO:0000313|EMBL:PZD95445.1, ECO:0000313|Proteomes:UP000249522}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMB1 {ECO:0000313|EMBL:PZD95445.1,
RC ECO:0000313|Proteomes:UP000249522};
RA Pinnaka A.K., Singh H., Kaur M.;
RT "Paenibacillus imtechensis sp. nov.";
RL Submitted (JUN-2018) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + S-adenosyl-L-methionine = [protein]-L-
CC glutamate 5-O-methyl ester + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:24452, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:10311,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:82795; EC=2.1.1.80;
CC Evidence={ECO:0000256|ARBA:ARBA00001541};
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:PZD95445.1}.
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DR EMBL; QKRB01000044; PZD95445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W1LKM7; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000249522; 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 GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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; 1.10.155.10; Chemotaxis receptor methyltransferase CheR, N-terminal domain; 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; IPR036804; CheR_N_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; 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:PZD95445.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000249522};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 22..211
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 217..463
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 854..905
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 928..980
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 993..1196
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 671..737
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 34
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1196 AA; 134601 MW; 9DFD591B9E40827D CRC64;
MQDQSADTAP GVNPSASRLD GSLSAPRIIG IGASAGGLEA LEQLIGHLPA DLGAAVIIVQ
HLSPDYKSFM SELLLRKTSM KVLEARSGMQ VMKNHIYLIP AKSYLTVHGG MLHLEDYPDQ
QGIHLPIDVF LESLAADQGS QSVGIILSGT GADGTSGVEA VHRAGGMVFV QDEETAKFNG
MPRSAIQTGI ADFVSSPAKI ADEIMMILQS PSPADTSEDQ LRKILTVIRK QSGIDFSSYK
QNGIIRRIER RMKIAGITSL RLYLEYMMDN MAEAVLLQKD LLIGVTHFFR DNEAFQTLVD
KVIPAICDTK LQNREKEIRI WVAGCSTGEE AYTIAMLFKQ YIDEQGIEIQ IRIFATDLDR
EAVDYAGIGV YPRHIEEHVP EPYLSKYFIP KEGSYQVSKD IRRMIVFAPH NIIKDPPFVN
LDLISCRNMM IYFQPYMQKK ILSLFHFALN TRGFLFLGPS ESIGKLDNLF KALDRKWNIF
CYKEVYQWSQ SQLKEVAYQD PDRETLSVLR SRESVLAGRQ EPAVQKLDDL NSQLAEELLP
PCVILNEKNE VIHTVGDVNK YIGMPKGRVS LNINKMVAAS LSMPLGTGIH KARREMQKVT
YANLKCGEGQ NGRSIKLTIQ PLFTKGEMRS LVAILFEEMM DRAVDAPAGA YHVYGANDDT
DYRILDLERE LQYTQDSLQA TIEELETANE ELQSTNEELI AANEEMQSSN EELQSVNEEL
ITVNSEHQRK IQELIELNND MDNFLLSTKI GTIFLDTDMC IRRFTPSAAE VFHLMEVDIG
RPIHHISHKL YYGSLIQDAA YVLATTDVVE KELQCSEGNW YSVRVLPYRT TDNLIRGVVV
TVVKITELKL ANKELQKLSY AIEQSPSMIM ITDVRGIIEY VNPVFIRKTG YKSEEIRDRS
LKDFLIETTS APQICSSIEK HIFTGDKWTG ELKQKTRDGE WYWETTSLLP IENEDGEIIH
YLKVSEDITE RKKTEELLRK SEMLSAVGEL AAGIAHEIRN PLTALKGFVQ LMKAQGGNET
YISIMLSEFD RIEHIINELL LLSKPKIINF QPQNLLMILN DVLLLIDTQA LLNKVTIHTE
LDAGHPYVHC VENQLKQVFI NLFKNAIEAM PEGGNIYVRV TRKDDGDIIM SIRDEGCGIP
ADKLPRLGEP FFTTKEKGTG LGLMVSYNII EGHNGVMRIQ SEEQKGTTIT IELPAL
//
