ID A0A0Q9L711_9BACL Unreviewed; 593 AA.
AC A0A0Q9L711;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ASG81_04215 {ECO:0000313|EMBL:KRE49585.1};
OS Paenibacillus sp. Soil522.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736388 {ECO:0000313|EMBL:KRE49585.1, ECO:0000313|Proteomes:UP000051180};
RN [1] {ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|Proteomes:UP000051180};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE49585.1, ECO:0000313|Proteomes:UP000051180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil522 {ECO:0000313|EMBL:KRE49585.1,
RC ECO:0000313|Proteomes:UP000051180};
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: 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:KRE49585.1}.
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DR EMBL; LMRV01000024; KRE49585.1; -; Genomic_DNA.
DR RefSeq; WP_056629529.1; NZ_LMRV01000024.1.
DR AlphaFoldDB; A0A0Q9L711; -.
DR STRING; 1736388.ASG81_04215; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000051180; 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 Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:KRE49585.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..587
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 593 AA; 67142 MW; 8662D37F47B34D3E CRC64;
MFAKLSRMLT DPFRRSIRNK LIFTMIILSV IPIIAVTLLA AENNRKSMEA EVIGTNLSNM
KWTGIHLGEQ FAQLNNLIYT VLISPHLSDY LASTEGASIY NQFAAQKNIL DTLNNLFYSA
GNHVIGVELY LKEPGKLFTI NASQNDLESS PVIPSPYKQL FEQNKDFVIR LTGAENGEFQ
LIRSINRFEN REKLGGISLV IRWSMLDQTL DLIGRGEEHK VLIAGEDGNI LYQPFGDKPS
QELMLRVKQT DDGQGYFRTP EEYVFYNTID PVGLKLVTIV PTSFINKSAQ STMHFGLIVG
GISVVVSIVI AFLLAWRTAT PIVNLARSMQ GLGIIKETEL PQSRRVDEIG LLETKLYNMS
YRIREHIKTE YSMNLEKKTA ELKALQAQIN PHFLQNTLQM IGSMLFTKKP AESYEIIRSL
SDMFRYVIRD PDDLATLKTE IEHLNNYMLI QKQRFSSRLS YTTDIDESAM RCAIPKLTLQ
PIVENAFFHG LENKTGDWQL NISVEREPNT VRIRIRDNGI GIRNDKLAEL RKRITNQSGQ
VWTQGDRIGI QNVASRIYMH FGPSYGIAID SEPGAGTTVT VTVPIESRGE QHD
//
