ID A0A3G9IL43_9BACL Unreviewed; 1055 AA.
AC A0A3G9IL43;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=Back11_03910 {ECO:0000313|EMBL:BBH19046.1};
OS Paenibacillus baekrokdamisoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1712516 {ECO:0000313|EMBL:BBH19046.1, ECO:0000313|Proteomes:UP000275368};
RN [1] {ECO:0000313|EMBL:BBH19046.1, ECO:0000313|Proteomes:UP000275368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33723 {ECO:0000313|EMBL:BBH19046.1,
RC ECO:0000313|Proteomes:UP000275368};
RA Kang S.W., Lee K.C., Kim K.K., Kim J.S., Kim D.S., Ko S.H., Yang S.H.,
RA Lee J.S.;
RT "Complete genome sequence of Paenibacillus baekrokdamisoli strain KCTC
RT 33723.";
RL Submitted (NOV-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};
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DR EMBL; AP019308; BBH19046.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9IL43; -.
DR KEGG; pbk:Back11_03910; -.
DR Proteomes; UP000275368; 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; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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; 1.
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:UP000275368};
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 23..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 445..663
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 715..831
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 673..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 764
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1055 AA; 118313 MW; F2DB9C57CFD83CE7 CRC64;
MGVVKGKMTM NVERIGMMSK RTLLFHIVPF VLLFIGIRVV WIVVEQPPDT PAAIRGELDL
RESNLNNDRT VSLGGEWEFY PNRFLMEKAN RTDISEEGNK FIQVPGNWGH SLSPLNDSNY
GYATYRLRIL VDPDDERLFS IRAKGIASSA ELYVNGRMLA SSSRSVGSVL YSTAFASKDG
RIDIVIQAAN YVNSQVGGIF DSVKFGTERA VSGEKQFSFA MQFMVLVVLA MHALYAMLIY
TFGARQKVLL SFTLLVLSAM FLVLADDDKL LRQWISLSWD WTIKLQILSL AGIGIFMLKF
TRELLLGHIP TRIYLPIQWL NTAAVLSVVL LPSSILLLTS SCVEVMMLLS ILVLLVLTIR
LVLSGVEDAI FLLFGVIAVI LSSLGGIVKN LGWFEMGFYP IDLLIAFLSS ASFWFKRYIR
AAAQTAILSE KLQREDKRKD DFLANVSHEL RNPLHGILNI AQSVLDSEKN VLGEKNVQNL
DLLVTVGRRM SFMLNDLLDL TLLKEKGIQL QVKAIHVQTV VSGVIDMLRF MTDGKRIRFD
NHIPKWFPLV MADESRLIQI LFNLLHNAVK YTNEGVITVR AHAEGGQATI FVQDTGIGME
DEQQRKIFEP YEQIDSGMTG GGNGIGLGLS ICKQLVELHG GMIKVHSVAD IGSTFFFTMK
LSSDSSTYWL ENDQKEKPET ADTADSEAAA ASAATNDFRE MMRKPLFKDD GDGPTILIVD
DDSVNLMVLD NILTVEGCKV VTASSGQEAL SVLDSREWDL IISDVMMPNM SGYELTRLIR
ERFTMSELPI LLLTARSRPE DLQTGFLSGA NDYVTKPMNA AELKTRVRAL TELKHSVRDQ
LRMEAAWLQA QIKPHFLFNT LNSIAALGDF DTTRMRSLLD VFGRYLKASF DFRNSERLVS
LEQELQLVQS YLYIEKERFE DRLQIRWDVD ESLMLYIPPL TIQTLVENAV RHGILKRTHG
GEIQIRVARI PGGAEVAIID NGVGMDANAV EKWLEGSSNP TTGIGLRNTD RRLKQIYGKG
LQIQSQPDQG TTVAFRIREK IFPSLFDTSS KEMKE
//
