ID A0A0Q3WL12_BRECH Unreviewed; 1029 AA.
AC A0A0Q3WL12;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AN963_18235 {ECO:0000313|EMBL:KQL47311.1};
OS Brevibacillus choshinensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX NCBI_TaxID=54911 {ECO:0000313|EMBL:KQL47311.1, ECO:0000313|Proteomes:UP000051063};
RN [1] {ECO:0000313|EMBL:KQL47311.1, ECO:0000313|Proteomes:UP000051063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8552 {ECO:0000313|EMBL:KQL47311.1,
RC ECO:0000313|Proteomes:UP000051063};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (SEP-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:KQL47311.1}.
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DR EMBL; LJJB01000010; KQL47311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q3WL12; -.
DR STRING; 54911.AN963_18235; -.
DR PATRIC; fig|54911.3.peg.1689; -.
DR Proteomes; UP000051063; 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; 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:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 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; 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:KQL47311.1};
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 204..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 434..653
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 687..804
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 916..1014
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 737
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1029 AA; 116912 MW; D4F592165A489F10 CRC64;
MLFIFFLSVV TFFVIYVKTV PVQNSPHAKN GVLDLSEWNF HDQGLANLDG EWEFYEGKLL
EPEDFRKGVR SDLGYLSVPG TWKGKNDDGS GMSRKGYGTY RLRVIVPESN QILGLKTRNI
RMSNQMFING NVEGNSGHPA ATLETHSPGN TPYTTYFYTE SREIEIVIQV ANYMYITGGI
INSIQFGLPE DITTLNGIQI GSDLAAVIIL VILGVYHLSF FFLRTKDKTY LYSGLYILTL
LMGQLVYGEK VLLRFMPQIP FDLAYKMQDL SVYISAIILM LFFYSIENRL MSLKKMLLMM
IPLFVYILAI LVLPYPVHSE YEYIYLVCME IILFYILGRM LYLYNLSRRD PAKKKEMVLF
IGASLCMLVV LTDGILYTEN IVPTDLMGKT AVIGFITCLN LLLAVRFTSA YEKTEILSHQ
LSVSNQLKDE FLTYTSHEMK TPLHGIQNIT AYLLEDEENP LSSEQQQNVW LIRDTSIKLS
MLIHDLIDVT RLKHGELRLS TTTVDVKVVT QMVFDVLQFE LVGKSVRLVN QIGSNVRVMA
DENRLRQIMY NLVHNAIKHT EAGTITVKAR VAEKEVSIYV EDTGTGIASE RHSSIFSYFD
QSDTPLPQDG YTSMGVGLYI SRKLIEQMDG QIQVDRSEVG KGTSMKFTLP RLEEAHMQQE
KAVAGTIQQR IVEDSLPLDI LNQPSHTIMI VDDEATNIQV LLHILKRHQY NVITAFSANE
ALLKMKEHPN VDLVILDVMM PEISGIELCK MLRVQNSIID LPILFATVKD TPHDIALGYR
AGANDYVTKP FDAETLIARI QTLIAMKTSI QEAIQNEYAF HQAQIKPHFL YNALSSVVSF
CYTDGKKAAY LLSMLSQYLR YILEMDRTTL YVPLYREMEL IEAYVEIEKA RFEDGFDFFC
HVDEECLNLH IPTLCIQPFI ENAIRHGLFE KVGQGNVSLM IHKRDGCIEV IIEDDGVGIA
TDLLERMNKG EQKNGSIGIL NIHKRLLSTP GSAMKIESEV GQGTRVYLSI PIRTEGMTEG
ERERRKMIV
//
