ID A0A090Y6R0_PAEMA Unreviewed; 616 AA.
AC A0A090Y6R0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DJ90_4883 {ECO:0000313|EMBL:KFM93512.1};
OS Paenibacillus macerans (Bacillus macerans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44252 {ECO:0000313|EMBL:KFM93512.1, ECO:0000313|Proteomes:UP000029278};
RN [1] {ECO:0000313|EMBL:KFM93512.1, ECO:0000313|Proteomes:UP000029278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8244 {ECO:0000313|EMBL:KFM93512.1,
RC ECO:0000313|Proteomes:UP000029278};
RA Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA Scholz M.B., Teshima H., Xu Y.;
RL Submitted (APR-2014) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KFM93512.1}.
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DR EMBL; JMQA01000052; KFM93512.1; -; Genomic_DNA.
DR RefSeq; WP_036627112.1; NZ_UGSI01000001.1.
DR AlphaFoldDB; A0A090Y6R0; -.
DR STRING; 44252.DJ90_4883; -.
DR GeneID; 77010235; -.
DR PATRIC; fig|44252.3.peg.6069; -.
DR HOGENOM; CLU_020473_6_1_9; -.
DR OrthoDB; 9776552at2; -.
DR Proteomes; UP000029278; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
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; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFM93512.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029278};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 309..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..382
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
SQ SEQUENCE 616 AA; 69034 MW; 4DF8A65029463CFC CRC64;
MSFRFKPLKS WSLRAKILLI FLLLISIPLS LQGVATYVDF SSSIERRTSD YTAQLVDQIN
RNLDRTLMEM QRLTLMPVYD SGVLSILRKY GGEDSLHQQP TVEERSKMQL YIASMTFDRP
EIDSIQIFAG SGYTFSSLAP SAIAAYTDVE GQPWYSRVEE ARGAWVLLPP HRPSYYLDGN
QSYFSVARLI REPNTNRTLG LVKIDLKQTL FKQLVDNARM EENGGIVVQN SREELFYTAP
AEKDTETSKL LPDRIRELSG RSETASQLLK MEGNEYLVVS NYSKYSDINI VSYIPVASLL
VETKELRNFT LLAGMVCLAL AGAFATYFSY RLTKPLGTLV RKMRLVELGD FKQSVPAVTE
DEIGRLGSGF NRMVEEIDRL VHEVYVLGMR EKEAELAALQ SQIHPHFIYN TLESISMLAR
QHGNEDVSEM TTALGRLIRS AVEQDQSLIR LGEELETAES YIHIQKMRHG SRLRAMFDIE
EGLDDFLVPK LLLQPLIENA IMHGIGDREQ GGTVYVTAAR FEDEVLLTIG DDGRGMSEEE
LAALRGLLEE AGAAAAKMPA TPLHGHGVAL KNIKQRLLLI YGSDCDFEID GSLGQGTAFT
ITLPFVTQKE QEVGIG
//
