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Database: UniProt
Entry: A0A0M2SWS6_9BACI
LinkDB: A0A0M2SWS6_9BACI
Original site: A0A0M2SWS6_9BACI 
ID   A0A0M2SWS6_9BACI        Unreviewed;       785 AA.
AC   A0A0M2SWS6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, 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=WQ57_14510 {ECO:0000313|EMBL:KKK37412.1};
OS   Mesobacillus campisalis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX   NCBI_TaxID=1408103 {ECO:0000313|EMBL:KKK37412.1, ECO:0000313|Proteomes:UP000034166};
RN   [1] {ECO:0000313|EMBL:KKK37412.1, ECO:0000313|Proteomes:UP000034166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA2-6 {ECO:0000313|EMBL:KKK37412.1,
RC   ECO:0000313|Proteomes:UP000034166};
RA   Mathan Kumar R., Kaur G., Kumar A., Singh N.K., Kaur N., Kumar N.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus campisalis sp. nov.,
RT   a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-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:KKK37412.1}.
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DR   EMBL; LAYY01000015; KKK37412.1; -; Genomic_DNA.
DR   RefSeq; WP_046524505.1; NZ_LAYY01000015.1.
DR   AlphaFoldDB; A0A0M2SWS6; -.
DR   PATRIC; fig|1408103.3.peg.3263; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000034166; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034166};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   DOMAIN          315..384
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          387..439
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          440..510
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          512..563
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          576..779
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   785 AA;  88354 MW;  649B84D92C50FDA4 CRC64;
     MAVHESNQKV KDKAISKTSI MLDIHAKMIH SITRGDSLPS IFEKLSRKLE QFWHGQVFCA
     VLWAARGDEH DIQSAPLLPE EIKSVLSIWK GGSREYFDGD MENDAIWKRI SKEALPFGLE
     GGWSIPILID GHIAGALALY QRESSLLEDE DLDFLQTLAK LAALAIQRDQ RLELEQILKE
     GEQKRLDREQ TAQHGELASL LKRHQGLIAK FQKVNGRFVY TNGAGQLFEK LGLNLVECIG
     KELKEIFPEP FCSKIEPYHN QAWNGNEVCY EGELYGIHYV AAFTPIFQEG QVTEVIISCN
     DVTELHRTSD DLSAAKEMLE AFVENSVDAI ATMDIEGRII FVNRSYSEMF GFKASEVIGK
     NIVDIQPDYE EELNEIFQKV ASGSNVNGYE TLRKRADGSL IAVSISHSPI RDKSGRITGV
     SGIIRDITEQ KRIEHELEES HQRYQSLFDS NPDLVASLDI DGRITNINPA VQKIIGYSAG
     QAKGKSYIEF VAPSTLEKSK IALRKALKGK PQTFEGELMQ KNGRKGLFHI THVPIIVTRK
     VVGIYVISKD ITAHKKAEEY LRKNDRISAI GQLAAGIAHE IRNPLTSLKG FIQLLEEKSD
     EKEYYRIMLR EMERLELITD EFLILAKPQA KKYSFKAISS ILEGFLPLVE TQANMNNVKI
     VTTMESGLPP ICCDVNQMKQ VFLNVMKNAI ESMPGGGEIS IDVKKKDDSI QIVIEDQGCG
     ISPRRLKRIW EPFYSTKEKG TGLGLMIIFN IIKEHRGDIE IQSELGKGTQ VRIMLPVTES
     QMTFQ
//
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