LIAS_BACSU
ID LIAS_BACSU Reviewed; 360 AA.
AC O32198; Q7B2J4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Sensor histidine kinase LiaS;
DE EC=2.7.13.3;
GN Name=liaS; Synonyms=yvqE; OrderedLocusNames=BSU33090;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9639930; DOI=10.1099/00221287-144-6-1593;
RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT chromosome containing genes involved in metal ion uptake and a putative
RT sigma factor.";
RL Microbiology 144:1593-1600(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION.
RX PubMed=11717295; DOI=10.1128/jb.183.24.7365-7370.2001;
RA Kobayashi K., Ogura M., Yamaguchi H., Yoshida K., Ogasawara N., Tanaka T.,
RA Fujita Y.;
RT "Comprehensive DNA microarray analysis of Bacillus subtilis two-component
RT regulatory systems.";
RL J. Bacteriol. 183:7365-7370(2001).
RN [4]
RP INDUCTION BY BACITRACIN.
RC STRAIN=168 / CU1065;
RX PubMed=14651641; DOI=10.1046/j.1365-2958.2003.03786.x;
RA Mascher T., Margulis N.G., Wang T., Ye R.W., Helmann J.D.;
RT "Cell wall stress responses in Bacillus subtilis: the regulatory network of
RT the bacitracin stimulon.";
RL Mol. Microbiol. 50:1591-1604(2003).
RN [5]
RP INDUCTION BY ANTIBIOTICS.
RX PubMed=15273097; DOI=10.1128/aac.48.8.2888-2896.2004;
RA Mascher T., Zimmer S.L., Smith T.-A., Helmann J.D.;
RT "Antibiotic-inducible promoter regulated by the cell envelope stress-
RT sensing two-component system LiaRS of Bacillus subtilis.";
RL Antimicrob. Agents Chemother. 48:2888-2896(2004).
RN [6]
RP INDUCTION BY STRESS.
RX PubMed=15856219; DOI=10.1007/s00253-005-1898-1;
RA Hyyrylaeinen H.-L., Sarvas M., Kontinen V.P.;
RT "Transcriptome analysis of the secretion stress response of Bacillus
RT subtilis.";
RL Appl. Microbiol. Biotechnol. 67:389-396(2005).
RN [7]
RP INDUCTION BY LL-37; PG-1 AND TRITON X-100.
RC STRAIN=168;
RX PubMed=15870467; DOI=10.1099/mic.0.27761-0;
RA Pietiaeinen M., Gardemeister M., Mecklin M., Leskelae S., Sarvas M.,
RA Kontinen V.P.;
RT "Cationic antimicrobial peptides elicit a complex stress response in
RT Bacillus subtilis that involves ECF-type sigma factors and two-component
RT signal transduction systems.";
RL Microbiology 151:1577-1592(2005).
CC -!- FUNCTION: Member of the two-component regulatory system LiaS/LiaR
CC probably involved in response to a subset of cell wall-active
CC antibiotics that interfere with the lipid II cycle in the cytoplasmic
CC membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also
CC involved in response to cationic antimicrobial peptides and secretion
CC stress. Activates probably LiaR by phosphorylation.
CC {ECO:0000269|PubMed:11717295}.
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 {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Induced, via LiaR, by antibiotics (vancomycin, bacitracin,
CC nisin and ramoplanin), cationic antimicrobial peptides (human LL-37 and
CC porcine PG-1), Triton X-100 and severe secretion stress.
CC {ECO:0000269|PubMed:14651641, ECO:0000269|PubMed:15273097,
CC ECO:0000269|PubMed:15856219, ECO:0000269|PubMed:15870467}.
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DR EMBL; AJ223978; CAA11744.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15299.1; -; Genomic_DNA.
DR PIR; F70045; F70045.
DR RefSeq; NP_391189.1; NC_000964.3.
DR RefSeq; WP_003244464.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32198; -.
DR SMR; O32198; -.
DR IntAct; O32198; 4.
DR STRING; 224308.BSU33090; -.
DR PaxDb; O32198; -.
DR PRIDE; O32198; -.
DR DNASU; 935967; -.
DR EnsemblBacteria; CAB15299; CAB15299; BSU_33090.
DR GeneID; 935967; -.
DR KEGG; bsu:BSU33090; -.
DR PATRIC; fig|224308.179.peg.3587; -.
DR eggNOG; COG4585; Bacteria.
DR InParanoid; O32198; -.
DR OMA; PLDIEWD; -.
DR PhylomeDB; O32198; -.
DR BioCyc; BSUB:BSU33090-MON; -.
DR Proteomes; UP000001570; Chromosome.
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 GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR017202; LiaS/VraS.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR PIRSF; PIRSF037431; STHK_LiaS; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..360
FT /note="Sensor histidine kinase LiaS"
FT /id="PRO_0000074780"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 69..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 74..126
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 153..346
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 159
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 360 AA; 40704 MW; B2DEE6E018B7AC7E CRC64;
MRKKMLASLQ WRAIRMTTGI SLLLFVCLIS FMMFYYRLDP LVLLSSSWFG IPFILILLLI
SVTVGFASGY MYGNRLKTRI DTLIESILTF ENGNFAYRIP PLGDDEIGLA ADQLNEMAKR
VELQVASLQK LSNERAEWQA QMKKSVISEE RQRLARDLHD AVSQQLFAIS MMTSAVLEHV
KDADDKTVKR IRMVEHMAGE AQNEMRALLL HLRPVTLEGK GLKEGLTELL DEFRKKQPID
IEWDIQDTAI SKGVEDHLFR IVQEALSNVF RHSKASKVTV ILGIKNSQLR LKVIDNGKGF
KMDQVKASSY GLNSMKERAS EIGGVAEVIS VEGKGTQIEV KVPIFPEEKG ENERDSSIID
