MALK_BACSU
ID MALK_BACSU Reviewed; 533 AA.
AC O05250; Q795M3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Sensor histidine kinase MalK;
DE EC=2.7.13.3;
DE AltName: Full=Malate kinase sensor;
GN Name=malK; Synonyms=yufL; OrderedLocusNames=BSU31520;
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=9274030; DOI=10.1099/00221287-143-8-2769;
RA Oudega B., Koningstein G., Rodrigues L., de Sales Ramon M., Hilbert H.,
RA Duesterhoeft A., Pohl T.M., Weitzenegger T.;
RT "Analysis of the Bacillus subtilis genome: cloning and nucleotide sequence
RT of a 62 kb region between 275 degrees (rrnB) and 284 degrees (pai).";
RL Microbiology 143:2769-2774(1997).
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 FUNCTION.
RX PubMed=12949159; DOI=10.1099/mic.0.26257-0;
RA Tanaka K., Kobayashi K., Ogasawara N.;
RT "The Bacillus subtilis YufLM two-component system regulates the expression
RT of the malate transporters MaeN (YufR) and YflS, and is essential for
RT utilization of malate in minimal medium.";
RL Microbiology 149:2317-2329(2003).
RN [5]
RP REGULATION OF MAEA.
RX PubMed=12949160; DOI=10.1099/mic.0.26256-0;
RA Doan T., Servant P., Tojo S., Yamaguchi H., Lerondel G., Yoshida K.,
RA Fujita Y., Aymerich S.;
RT "The Bacillus subtilis ywkA gene encodes a malic enzyme and its
RT transcription is activated by the YufL/YufM two-component system in
RT response to malate.";
RL Microbiology 149:2331-2343(2003).
CC -!- FUNCTION: Member of a two-component regulatory system MalK/MalR.
CC Involved in the activation of maeA, maeN and yflS in presence of
CC malate. Probably activates MalR by phosphorylation.
CC {ECO:0000269|PubMed:11717295, ECO:0000269|PubMed:12949159}.
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}.
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DR EMBL; Z93937; CAB07946.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15141.1; -; Genomic_DNA.
DR PIR; A70009; A70009.
DR RefSeq; NP_391030.1; NC_000964.3.
DR RefSeq; WP_003228835.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O05250; -.
DR SMR; O05250; -.
DR STRING; 224308.BSU31520; -.
DR PaxDb; O05250; -.
DR PRIDE; O05250; -.
DR EnsemblBacteria; CAB15141; CAB15141; BSU_31520.
DR GeneID; 937173; -.
DR KEGG; bsu:BSU31520; -.
DR PATRIC; fig|224308.179.peg.3417; -.
DR eggNOG; COG3290; Bacteria.
DR InParanoid; O05250; -.
DR OMA; HYQNGWL; -.
DR PhylomeDB; O05250; -.
DR BioCyc; BSUB:BSU31520-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; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; IPR000014; PAS.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR033463; sCache_3.
DR InterPro; IPR029151; Sensor-like_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR InterPro; IPR039506; SPOB_a.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF17203; sCache_3_2; 1.
DR Pfam; PF14689; SPOB_a; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR SUPFAM; SSF55890; SSF55890; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
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..533
FT /note="Sensor histidine kinase MalK"
FT /id="PRO_0000074804"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 210..281
FT /note="PAS"
FT DOMAIN 335..527
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 338
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 533 AA; 58930 MW; 9CDF9A58EFD5AA10 CRC64;
MKKTLKLQTR LTIFVCIVVL IALLITFFTV GAQTTKRIRD QEKATALQTA EMVAEAPMTA
AALESGKKQK ELQSYTKRVQ KITGTEFVVV MDMNGIRKTH PDPSKIGKKF RGGDESEVLK
GHVHISTASG TLGKSQRAFV PVYAENGKQV GAVAVGITVN EIDEVISHSL RPLYFIICVS
IFVGVIGAVI VARTVKNIMY GLEPYEIATL LEERSAMLES TKEGILAVDE HGKIKLANAE
AKRLFVKMGI NTNPIDQDVD DILPKSRLKK VIETKKPLQD RDVRINGLEL VFNEVPIQLK
GQTVGAIATF RDKTEVKHLA EQLSGVKMYA NALRAQSHEF MNKLHVILGL VQLKEYDDLG
DYIKDIAIQQ KSETSEIIND VKSSVLAGFL LGKQSFIREQ GANLDIECNG VIPNAADPSV
IHELITIIGN LINNGLDAVA DMPKKQITMS MRFHNSILDI EITDTGAGMS EEDQAKVFEQ
GYSTKGKNRG FGLYFTQQSI ENLKGQMILT SEKNEGTTFS IRIPYEPKEE NHD
