GenomeNet

Database: UniProt
Entry: A0A160F5H8_9BACI
LinkDB: A0A160F5H8_9BACI
Original site: A0A160F5H8_9BACI 
ID   A0A160F5H8_9BACI        Unreviewed;       593 AA.
AC   A0A160F5H8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-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=GFC30_2157 {ECO:0000313|EMBL:ANB61686.1};
OS   Anoxybacillus amylolyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=294699 {ECO:0000313|EMBL:ANB61686.1, ECO:0000313|Proteomes:UP000076865};
RN   [1] {ECO:0000313|EMBL:ANB61686.1, ECO:0000313|Proteomes:UP000076865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15939 {ECO:0000313|EMBL:ANB61686.1,
RC   ECO:0000313|Proteomes:UP000076865};
RX   PubMed=16682297; DOI=10.1016/j.syapm.2005.10.003;
RA   Poli A., Esposito E., Lama L., Orlando P., Nicolaus G., de Appolonia F.,
RA   Gambacorta A., Nicolaus B.;
RT   "Anoxybacillus amylolyticus sp. nov., a thermophilic amylase producing
RT   bacterium isolated from Mount Rittmann (Antarctica).";
RL   Syst. Appl. Microbiol. 29:300-307(2006).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP015438; ANB61686.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A160F5H8; -.
DR   KEGG; aamy:GFC30_2157; -.
DR   PATRIC; fig|294699.3.peg.2225; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000076865; Chromosome.
DR   GO; GO:0005886; C:plasma 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   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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   InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR   PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR   PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR   Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076865};
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};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        116..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          449..578
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   593 AA;  65626 MW;  D1108EA7F31B8C23 CRC64;
     MWQLCLSMVE RLGIIVMVAF LLTRLSYFRR LIYHQQVDWT QRFIIMVIFG IFGIVGTYTG
     LTVHVETFEV AKWTWSLKEN EALANSRVIG VVIAGLLGGW QVGLGAGLIA GVHRLFLGGF
     TAVACGVSTI IAGAIAGMVH HHKKRAFALS PEVALVVGMA AETLQMLVIL LVAKPFDRAL
     LLVEEIGVPM VIANGLGSAI FILVIRNVFQ EEEKAGALQA EKAMRLAEAT IHHLRNGLTP
     QSAKAICELF IQEVPSVAVS VTDRAHILAH VGAGSDHHFA NEPIQTETTR RVVETGEMLI
     VHDRVACHDP HCPLHKAIIA PLKRKDETVG TLKFYFQSEA DLSSITFEFV KGLSSLLSLQ
     LEIAEAEKYY QLMKEAQIKA LHAQVHPHFL FNALNTIVSC IRIDPNRARQ LLVSLAYYFR
     KNLAGTTEML STLEEEIRHV QAYLTIEEAR FQDKLRVRYD IEEGFDRVVL PTMTLQPLVE
     NAVKHGLKYM KKGSEIVIVV KADRDMVKIS VSDNGKGMTD EEVAQLLRTP VASSKGAGIG
     LYNVYERIKS LLGEEAKFAI VSAKGKGTTV QLTVPLKEGK EGDVVAYASY RRR
//
DBGET integrated database retrieval system