ID U1YE60_ANEAE Unreviewed; 1047 AA.
AC U1YE60;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF0083_01539 {ECO:0000313|EMBL:ERI10372.1};
OS Aneurinibacillus aneurinilyticus ATCC 12856.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=649747 {ECO:0000313|EMBL:ERI10372.1, ECO:0000313|Proteomes:UP000016511};
RN [1] {ECO:0000313|EMBL:ERI10372.1, ECO:0000313|Proteomes:UP000016511}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12856 {ECO:0000313|EMBL:ERI10372.1,
RC ECO:0000313|Proteomes:UP000016511};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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:ERI10372.1}.
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DR EMBL; AWSJ01000101; ERI10372.1; -; Genomic_DNA.
DR AlphaFoldDB; U1YE60; -.
DR STRING; 649747.HMPREF0083_01539; -.
DR PATRIC; fig|649747.3.peg.1393; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2972; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_011115_1_0_9; -.
DR Proteomes; UP000016511; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
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; 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; 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, ECO:0000313|EMBL:ERI10372.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; 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 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 382..403
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 457..675
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 721..837
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 948..1047
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 770
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1047 AA; 118807 MW; AD6D5B61AFE06BF7 CRC64;
MYLSYIKVEL RSQVLLNNLI RIKKWKIFLL VGLFLVVLTG SRILWMISFQ STEQPHVVNG
QLDLRNWDAT EGCTITLDGQ WEFYPHTWLM SNGNHKEPVR GNPEFIQVPG NWNASLQPGH
NTPYGYGSYR LRILVNPEND LTYSIRIPSV RSSSALYVNG RLLAKSGHPG ATEEEYVAWN
VPYSASFTTN GSNIIEVVIQ AANYKDPRNS GIVRSLKFGT EDAIARETQL SVSMQQMVAV
VFLLHAVYAL ILFLVGNREK RLLYFSLLIV SAMLINLLGS EEKLLLYWLP IDYELGFKLV
HLSMIVVAYC LLQCVVHELP TCWFKIFPWY VILCGAAVLW LLLPSQYIVT LQPLYVMIIG
ISILIAIVSI LYTSMKNIED NVLLLLSLVA FTNSLVWWGV LLITGIKIVY YPFDLIVSMT
CFASVWFRRY FQVHFETKNL AAKLQRVDKL KDEFLANTSH ELRNPLHGIL NISQAVLERE
QHSLNEKSVK DLETVLSVGR RMTLMLNDLL DVMSLKESNP KLKMRVLSIQ TIATGALDML
HFMTEGKPIQ LINHIPEEFP KVFADENRVI QIVFNLLHNA VKYTNEGEIS IRGYVKDGRA
HIAISDTGIG MDEETMRRVF EPYEQADPGK TMIEGGFGLG LSISKQLVEL HGGTLQVSSV
LGHGSEFTFT LQLADPAILQ EETETKIHTS IAFTEAALAA SVPPFDSISG QQPQILTDRP
RILVVDDDPV NLKVLETVLS SEQFDIMTVT SGKKALAVLD SKEWDLVISD VMMPQMSGYE
LSRTIRRQFT ITELPILLLT ARSQPEDIEN GFLSGANDYV TKPVDALEIR ARVRTLTEVK
QSVREQLRME AAWLQAQIQP HFLFNTLNTV YALSEIDMDR MRNLLEAFSN FLRDKFKFQS
ADELVPIEEE LSIVRSYLYI EKERFDDRLQ VTWEISGCKQ LKIPLLTIQP LVENAVRHGI
MKRARGGNIH IRLSDYETYA KIVVADDGVG MDEEMVQRIF MKQSDTTSGI GLSNTDRRLK
RHFGRGLQIT SKPGYGTSIS FIVYKNK
//
