ID A0A0F5R6R6_9BACL Unreviewed; 1198 AA.
AC A0A0F5R6R6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=VE23_13920 {ECO:0000313|EMBL:KKC47954.1};
OS Paenibacillus sp. D9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC47954.1, ECO:0000313|Proteomes:UP000036611};
RN [1] {ECO:0000313|EMBL:KKC47954.1, ECO:0000313|Proteomes:UP000036611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D9 {ECO:0000313|EMBL:KKC47954.1,
RC ECO:0000313|Proteomes:UP000036611};
RA Sharma V., Lin J.;
RT "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT sp. D9, isolated from diesel contaminated soil.";
RL Submitted (MAR-2015) 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:KKC47954.1}.
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DR EMBL; JZEJ01000001; KKC47954.1; -; Genomic_DNA.
DR RefSeq; WP_048744945.1; NZ_JZEJ01000001.1.
DR AlphaFoldDB; A0A0F5R6R6; -.
DR PATRIC; fig|665792.3.peg.3099; -.
DR OrthoDB; 9816309at2; -.
DR Proteomes; UP000036611; 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; 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: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; PF08448; PAS_4; 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; 2.
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:KKC47954.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000036611};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 14..198
FT /note="CheB-type methylesterase"
FT /evidence="ECO:0000259|PROSITE:PS50122"
FT DOMAIN 212..468
FT /note="CheR-type methyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50123"
FT DOMAIN 809..859
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 856..903
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 929..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 REGION 506..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 659..728
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 510..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 147
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00050"
SQ SEQUENCE 1198 AA; 134669 MW; 745A5540234D2F01 CRC64;
MNKIPSDSQH SELPLTKAEP VRIVGIGASA GGLEGLKHFF QQASPETGLA FVVIQHLSPD
HKSLMNEILS LYTRMQIHLV RDGMEVEPNT IYLVPPRKSL SLKKNHLWLS DPHPDEVHYP
IDYFFHSLAA DQGQQAIAVV LSGTGTDGTR GIAAVKRSGG IVFAQNEESA KFDGMPRSAI
DSGHVDFVLA PEKIASKLKF PASLIPSPSY AVQAAALNDS EALLAKILER VRERTNIDFS
FYKKNSLLRR IEKRMAEAGA ATLADYELLL ESREEEVLAL RQDLLIHVTH FFRDPEAFDI
IREKVLPKLV RAKLQNKNTE LRIWTAGCST GEEAYSIGML ALEVLEQEGL QNRFSIRIFA
TDVDKQSIDY ANHGVYPLSI GTSVSKARLD KYFVRHGDTY QVTRELRRLI VFAPHNLTKD
PPFSNLDLIS CRNMLIYLQP EMQQKVLSLF NFALTPGGFL FLGPSETVGR QDHLFEPSNG
KWNIFRHKSQ RKNSASGATL LMDGARSLST PGELRERRKQ HAGADAQENR RQSQFYSTYV
NEHMAPSLLV DEKLDIQHLT GNVQPFLSPM EGRPSWNLQK MLEPGLAVAV MTAVQQIRAG
LDEVVFRHLV VQTASGEQRI NVTVRPFSKS GAAFAGSMLI ILELAPELDE VPVASIDLND
SVRRQMVWLE QQLRSTEDKL QSAIEELEAS NEELQSTNEE LIASNEELQS TNEELQAVNE
ELVTINSEYQ FKIQELTELN NDMDLFLVST KIGTIFLDTQ FCIRRFTPAV TKEIHLLNVD
IGRPFHHISH QFYYDQFVED ASRVLQSLRS LEKEIKSRSG RWYKMRMMPY RTLEHLTKGV
IITLVDITEL KEANEELLRL SYAIEQSPIL VVISDLEGGI LYANRQFHDL TGETSESIYG
RHLESLDDWQ ASGCSFADIW EKLKRGEIWE GELAGIGRDG AVYWEQARLL PIVKRGETIH
YMKISENITD RKTTEEMLRK SEMLGAVGQL AAGIAHEIRN PLTSLKGFTK LMQEDNRRNY
ISIMAMELER IEQIVSELLV LSKPQAVDFH PVALGAVLRD VVMLIEAQAI MNNVQLELEI
PESDMLVQGV DNQLKQVFIN LIKNSIEAMS SGGVIQVKAS VGEDNMAWTR IIDQGSGIPP
EKLAKLGEPF FSTKAKGTGL GLVMTYKIVE NHHGKMYYES ELGKGTTGFV GLPIIRSS
//
