ID A0A0Q4RD21_9BACL Unreviewed; 1033 AA.
AC A0A0Q4RD21;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASF12_31000 {ECO:0000313|EMBL:KQO12444.1};
OS Paenibacillus sp. Leaf72.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736234 {ECO:0000313|EMBL:KQO12444.1, ECO:0000313|Proteomes:UP000051722};
RN [1] {ECO:0000313|EMBL:KQO12444.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO12444.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO12444.1, ECO:0000313|Proteomes:UP000051722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf72 {ECO:0000313|EMBL:KQO12444.1,
RC ECO:0000313|Proteomes:UP000051722};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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:KQO12444.1}.
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DR EMBL; LMLV01000009; KQO12444.1; -; Genomic_DNA.
DR RefSeq; WP_056035649.1; NZ_LMLV01000009.1.
DR AlphaFoldDB; A0A0Q4RD21; -.
DR STRING; 1736234.ASF12_31000; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000051722; Unassembled WGS sequence.
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; cd00156; REC; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000051722};
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 206..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 434..651
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 699..816
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 927..1024
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1033 AA; 116551 MW; 332BDEFE6F94F492 CRC64;
MKNKALFGML GFILLLLIGA NVASQLKWDD QPEARNGVLD LSKWDGVGQK VIKLKGEWDF
YPKQLWGDMA EAKTGPLSKQ AHVPGNWSNM LLNMYDSQAF GYGTYHLRIQ FGEHQPELQA
FQVPLIRSAH RLLINGEEIG ASGALDDGLK QYKGKIKPYI AYTQIRTDSI DIFVQVANFD
HATSGGIIQA IRMGPPDLIV QEQQQFAAFE FGTIAFFIVF GLYFGVLHLQ DRGSGWIYLS
FFFLCTALLN SVQGTRWLLA IWPEMPYRMT VTVYWLCSIS ILVGMFMYLA VRHEQRVNRL
FKRGLLVISS AMAACILVMP TAISTRLLPL WLMVSFIVHI YILLVVLRNL RSGDEQNRYE
FWSFCLFSAQ ALLNSLVLFG FGELTLWYFV QMIGFSIAIS YLFLHQFFRA YQKNEALTLE
LHRVNRFKSE FMTGISEQMI TPLNAMIGVA EARLHADESL SMEQIHDLRL ITSVGWTMRR
LVDDMMDFAR LLEAGIALTV RPIHLPSVVG EVIERTRYLV FSDSITLMNT IPQGLPPIVA
DEQRLQQILT GLIQSALKLT IEGTITTKAS VLSNRMELEI IMQGTGITDD TAATLVKMLH
LEDEASRPLP YDEHLGLFLV HALVKLHQGR ISVASGLAQE VVIGLSLPIA IELLAGSSAG
SFPEFHGNSV DLSLQAQGLV DQRLRSRKLY ESQETERAEI LIVSDDSLNI NVLVKLLAMD
QYRVTVVKKG REALKRLHHM RDTDLVIVER ILQDMSGLDV CRNIREHFTS FELPILLMTS
AGYSDHAIAA SQAGANDFLV KPVEWSELRV RILTLVQLKR SVGARIQMEL AFLQAQIKPH
FLFNTLNSIA ALSKKQPEKM TDLLTEFGHY LRESFRFDSS EPLVPFEREL KLVKSYLHIE
KVRFEDWLTF DIQVMTELSF WIPPLTIQPL VENAVRHGIM RRADGGHLEI CVWQEGGDIL
ITVKDNGVGM PAELPPHAEA APLTGGIGLA NIDRRMKQLF GYGLTISSRP GEGTEIRIRL
PMEKVGIHES YTG
//
