ID A0A160FA91_9BACI Unreviewed; 1017 AA.
AC A0A160FA91;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=GFC29_3246 {ECO:0000313|EMBL:ANB63501.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB63501.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB63501.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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};
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DR EMBL; CP015436; ANB63501.1; -; Genomic_DNA.
DR RefSeq; WP_044746209.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A160FA91; -.
DR KEGG; anl:GFC29_3246; -.
DR PATRIC; fig|1490057.3.peg.3566; -.
DR OrthoDB; 9809348at2; -.
DR Proteomes; UP000076753; Chromosome.
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:SF83; HISTIDINE KINASE; 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:ANB63501.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000076753};
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 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 360..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 434..652
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 693..809
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 919..1017
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT MOD_RES 742
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1017 AA; 115982 MW; CDD2390D00C3D293 CRC64;
MSKRKIAFIL SVFLLIIIMI RFLWMSAFTI PDHPTAERGV LDLRGWEPLK EHSLPLDGEW
EFFPNQWLIT KQGKSVVSSK EVQWIRVPGN WRTSTENGQV FGYGSYRLRI LLDPHQEAIY
GIHIPSISSS AEVYVNGKLL SQAGIPASEK ESYQPRTTPQ TVYFPVNHAT KIELIIQVAN
YDHPFRAGIL QSVHLGLLEP LSQEIQFNTT VAIITCVIYL FHALYSLIVF LIGNRNKTFL
YFSLMILCIV NGTLIGNGLL FQWVPLSFEW SIKITLLTMV AGGYTLLKCI QHFLPDKLQT
KVPPLYYLLC TITVLMIFSF PISIHLTWQW YYIFMMLIPC LLAPLALYRA TTRINDDNIF
LFLAIIAAVG SLIWFVVIFI FSIEMKSYPF DLMIAMICFS TYWFKQYFRT FSESQELTKK
LQKADKQKDE FLTSVAHEMR NPLHGMINIS QAVLENEKAH LRANSAKHLE LMVSIGRHMS
TLLDALLDLE RLKENRIKMK RRLLSLYDVT ETVLDMIRFL TDEQSIRLVN RVPANLPPVF
ADENRVIQIL FNLLHNAVKY AQADEVSVHA SIQGDWVNVS VVDTGIGIHE TLLDTIFERY
TQGNAESAAM ENGVGLGLHI CKQLVELHGG TLTVHSTPGQ GSVFTFSLEL ANTEHPKEEK
VQDSTKIPVL SKTDTAKQQQ ALDKSLPNQG SVRILAVDDD PINLRILEII FSEAPYHVVS
VTSSQEALAL VESEEWDVVI ADVMMPYMSG YELTRMIRQR ASNFELPILL LTARSHPEDI
VAGFLAGAND YVTKPIEGLE LKARVNTLIH LKQSIHERLR MEAALLQAQI HPHFLFNTID
TIASLSTIDH DRMIHLLVEF GNYLRKSFDS ENFQKLVPLE HELELLRSYL YIQKERFGDR
LTIDWDIDQH LHVLIPPLII QPLVENAIRH GILQRIHGGT VQIRIIDQGK HVEVTIADNG
VGMTEEEIRK ILHTTCQTKG IGIYNTNWRL KQLFGEELHI KSTPGEGTTI FFKIPKT
//
