ID E3ED98_PAEPS Unreviewed; 1046 AA.
AC E3ED98;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=ywpD {ECO:0000313|EMBL:ADO54455.1};
GN ORFNames=PPSC2_02415 {ECO:0000313|EMBL:ADO54455.1};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO54455.1, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO54455.1, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO54455.1,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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; CP002213; ADO54455.1; -; Genomic_DNA.
DR RefSeq; WP_013369095.1; NC_014622.2.
DR AlphaFoldDB; E3ED98; -.
DR STRING; 1406.LK13_15180; -.
DR KEGG; ppm:PPSC2_02415; -.
DR PATRIC; fig|886882.15.peg.465; -.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_011115_1_0_9; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000006868; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR008979; Galactose-bd-like_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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF02518; HATPase_c; 2.
DR Pfam; PF06580; His_kinase; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 2.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 228..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 451..669
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 714..831
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 942..1040
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 764
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1046 AA; 116623 MW; FB1FA6F7B2FED1D5 CRC64;
MKKQGVLFFI ILLLAVALPV YPLVSGVLSG NSHWKAHNGV IDLRNWDPDK EGAVQLGGEW
EFYPNQLFQP SSFQETRYQD WGNRQNSSKL GLGTGSSAKI VDVPGKWNQW MPGGQATGYG
TYHVRVLLPE KVENLYGIHM QNIRNSSRVW INGAEVGASG IPSVSADKGK QGNAPFVGFA
AVDGHSADIT VHVANYSYSS GGIIYPLLFG DYASITHSRE VAMAEDTVLV AGFFIPTVFF
IMLYFLRRKE KALLYLACFC IAALFYILTH GEKLLVWGMP DLPYEWILKI QSFSSTLFYY
FLIRYVHLTT QIVMNRIVLL LYNIVTALML GMGLLLPTLV LSSFETFILL FGVVSVGYVL
LILIRGLLQR TDDAALLVIS IMSILMIVVT SFVYVLGWGD VRGVTAYEML IFVLAQTLLL
AKRFVHSFME VENLSRRLLT LDGLKDEFLA NTSHELRTPL HGIINIAQSM LDRYGAQFNE
PQKHNLALIV NVGRRLSYLI NDILDFSNLK NGRLALNRRP VNVQTAVNSV LEVLGHNVGK
KKLQFVKEWP NSLPKVDADE DRLNQILYNL LGNAMKFTEE GEIVISAKVR NREMEISVKD
TGPGIAPDHL SHIFEPFNRG ANAEDKGYSG TGLGLGITRR LVELHGGYIR VESRLGKGST
FYFTLPLAET GTSAHEVQKD VLSEVILKPG VTSNQGVNPL EEDGLEQVRN VPYRVLAVDD
DGVNLRVLEE LLYATGCSVV AVDHAEEALQ LLNGRARFDL VITDWMMPEM SGIELCRRIR
EGYSLSELPV LLLTARDLPG DIHAGFMAGA NDFLRKPVDA EELKARVRTL LNMRNSAEEA
VRSEMAFLQA QIKPHFLYNA LNVIVSTVAV DPDKAAELLM ELSQYLRGSF DFQNRENTVP
LCKELELVES YVALEKARFE ERLQVTIEVG RNIRSLIPPL SIQPIVENAI RHGVMQRATG
GTVRVIVQED GADFVVSVTD DGVGIPPERL QQLLSEEHVS SSVGLRNIHR RLIHMYGEGL
RIESNPMQGT TVSFRVPETI LSHPTE
//
