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Database: UniProt
Entry: A0A2A8SGN0_9BACI
LinkDB: A0A2A8SGN0_9BACI
Original site: A0A2A8SGN0_9BACI 
ID   A0A2A8SGN0_9BACI        Unreviewed;       589 AA.
AC   A0A2A8SGN0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CN326_05450 {ECO:0000313|EMBL:PEZ08520.1};
OS   Bacillus sp. AFS018417.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033491 {ECO:0000313|EMBL:PEZ08520.1, ECO:0000313|Proteomes:UP000220085};
RN   [1] {ECO:0000313|EMBL:PEZ08520.1, ECO:0000313|Proteomes:UP000220085}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS018417 {ECO:0000313|EMBL:PEZ08520.1,
RC   ECO:0000313|Proteomes:UP000220085};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) 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:PEZ08520.1}.
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DR   EMBL; NTTM01000009; PEZ08520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A8SGN0; -.
DR   OrthoDB; 9776552at2; -.
DR   Proteomes; UP000220085; Unassembled WGS sequence.
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   CDD; cd16957; HATPase_LytS-like; 1.
DR   Gene3D; 1.10.1760.20; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003018; GAF.
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; 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; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF06580; His_kinase; 1.
DR   SMART; SM00065; GAF; 1.
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   Kinase {ECO:0000313|EMBL:PEZ08520.1};
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:UP000220085};
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        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        87..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          473..577
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   589 AA;  65294 MW;  321CF8E340A100A0 CRC64;
     MGDLLLMMIE RVGLIVILGY LLSHIKAFRW LLYKQDSYKG SFMLIGIFSL FTIVSNYTGI
     EISGNTIMND NWLRGVSSSS TIANTRIMGI GISGLLGGPI VGIGVGLIAG IHRYMLGGTT
     ALSCAISSIL AGVVTGYIGY LYQKRNRVVT PKFSAVLSIC MVSLEMIMIL FMIDDGWSIV
     KTIAIPMILV NGFGSFILLS MIQSILRQEE HAKALQTHKV LRIADKTLPY FRQGLTEESC
     THVAQIIHSF TGTDAVSLTD TEKILAHVGL GSDHHIPSHS LITELSKEVL KTGKIMKAKS
     REEINCQHEE CLLQAAIVIP LTSRGKTIGT LKLYFKNPNS LSPVEEELAE GLAKIFSTQL
     ELGEAELQSK LLQDAEIKAL QAQINPHFLF NAINTVSALC RTDVEKARKL LLQLSVYFRC
     NLQGARQLLI PLEQELNHVH AYLSLEQARF PNKYEVKMYI EDELHNILLP PFVLQLLVEN
     ALRHAFPKKQ PLCQVEIHVY AKKNSVHFKV KDNGQGIEPE RLEQLGKAIV SSKKGTGTAL
     YNINERLMGL FGKDTTLHIV SELEAGTEIS FTIPIQRKGG SDIENISSR
//
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