ID   SPAK_BACIU              Reviewed;         459 AA.
AC   P33113;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Sensor histidine kinase SpaK;
DE            EC=2.7.13.3;
DE   AltName: Full=Subtilin biosynthesis sensor protein SpaK;
GN   Name=spaK;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=8439156; DOI=10.1128/aem.59.1.296-303.1993;
RA   Klein C., Kaletta C., Entian K.-D.;
RT   "Biosynthesis of the lantibiotic subtilin is regulated by a histidine
RT   kinase/response regulator system.";
RL   Appl. Environ. Microbiol. 59:296-303(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX   PubMed=8085823; DOI=10.1128/aem.60.8.2793-2801.1994;
RA   Klein C., Entian K.-D.;
RT   "Genes involved in self-protection against the lantibiotic subtilin
RT   produced by Bacillus subtilis ATCC 6633.";
RL   Appl. Environ. Microbiol. 60:2793-2801(1994).
RN   [3]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Klein C.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Member of the two-component regulatory system SpaK/SpaR
CC       involved in the regulation of the biosynthesis of lantibiotic subtilin.
CC       SpaK may function as a membrane-associated protein kinase that
CC       phosphorylates SpaR in response to environmental signals.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA22781.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L07785; AAA22781.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U09819; AAB91593.1; -; Genomic_DNA.
DR   PIR; I40519; B48965.
DR   AlphaFoldDB; P33113; -.
DR   SMR; P33113; -.
DR   DIP; DIP-48345N; -.
DR   IntAct; P33113; 1.
DR   BRENDA; 2.7.13.3; 658.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16975; HATPase_SpaK_NisK-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
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; IPR008358; Sig_transdc_His_kin/Pase_MprB.
DR   InterPro; IPR044082; SpaK_NisK-like_HATPase.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR01780; LANTIREGPROT.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW   Two-component regulatory system.
FT   CHAIN           1..459
FT                   /note="Sensor histidine kinase SpaK"
FT                   /id="PRO_0000074879"
FT   TOPO_DOM        1..18
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        40..155
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..459
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          244..458
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT   MOD_RES         247
FT                   /note="Phosphohistidine; by autocatalysis"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ   SEQUENCE   459 AA;  52457 MW;  0F24A4710FA0BF4E CRC64;
     MGIGFKGRKT LLRELVKYMV TLCISLVVLA LLYIFINTIA MNTGFSHPAN YNEREAEKLA
     PKLETIDKVT ADMIPDTMSY AILNKETKQK TAGTIKEKDL QLVKKKIEKK PYVNYKQKGY
     LVIERNNEYC VLQYSLRADF SSPLLRKYLP NYELTSICIL IILLIIVISI ITTYFANRLR
     KHFETLNVIT RYIKEQNLQF TPEFTHIKEF DDVIDSLIEM RDALQSSLEA LWRLEKNKKE
     QIGALAHEIK IPITIIKGNA ELLSLSMQNE EQAEYTKYIL GAGNQIEQYI YQLIHLSKTE
     DALTIHLEKA SVDELTETLV KDISAYKGNK NINISFKKEN LMKEAKIDWQ LLHRALLNIL
     TNAVDYTPEG GTVSVHAECD SEIFYFFVKD TGNGFSEMGL KKATELFYMD DKSRHSKGHY
     GMGLTFAKNA VNLHNGELTL GNTIAGGAEV RVKIPLRNE