RESE_BACSU
ID RESE_BACSU Reviewed; 589 AA.
AC P35164;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Sensor histidine kinase ResE;
DE EC=2.7.13.3;
GN Name=resE; Synonyms=ypxE; OrderedLocusNames=BSU23110;
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 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=7934829; DOI=10.1111/j.1365-2958.1993.tb02670.x;
RA Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.;
RT "The organization of the Bacillus subtilis 168 chromosome region between
RT the spoVA and serA genetic loci, based on sequence data.";
RL Mol. Microbiol. 10:385-395(1993).
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=8631715; DOI=10.1128/jb.178.5.1374-1385.1996;
RA Sun G., Sharkova E., Chesnut R., Birkey S., Duggan M.F., Sorokin A.V.,
RA Pujic P., Ehrlich S.D., Hulett F.M.;
RT "Regulators of aerobic and anaerobic respiration in Bacillus subtilis.";
RL J. Bacteriol. 178:1374-1385(1996).
RN [4]
RP SUBUNIT, INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=25909364; DOI=10.1371/journal.pgen.1005140;
RA Schneider J., Klein T., Mielich-Suess B., Koch G., Franke C., Kuipers O.P.,
RA Kovacs A.T., Sauer M., Lopez D.;
RT "Spatio-temporal remodeling of functional membrane microdomains organizes
RT the signaling networks of a bacterium.";
RL PLoS Genet. 11:e1005140-e1005140(2015).
RN [5]
RP INTERACTION WITH FLOT.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=26297017; DOI=10.1099/mic.0.000137;
RA Schneider J., Mielich-Suess B., Boehme R., Lopez D.;
RT "In vivo characterization of the scaffold activity of flotillin on the
RT membrane kinase KinC of Bacillus subtilis.";
RL Microbiology 161:1871-1887(2015).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=27362352; DOI=10.1371/journal.pgen.1006116;
RA Dempwolff F., Schmidt F.K., Hervas A.B., Stroh A., Roesch T.C., Riese C.N.,
RA Dersch S., Heimerl T., Lucena D., Huelsbusch N., Stuermer C.A.,
RA Takeshita N., Fischer R., Eckhardt B., Graumann P.L.;
RT "Super Resolution Fluorescence Microscopy and Tracking of Bacterial
RT Flotillin (Reggie) Paralogs Provide Evidence for Defined-Sized Protein
RT Microdomains within the Bacterial Membrane but Absence of Clusters
RT Containing Detergent-Resistant Proteins.";
RL PLoS Genet. 12:e1006116-e1006116(2016).
CC -!- FUNCTION: Member of the two-component regulatory system ResD/ResE
CC involved in the global regulation of aerobic and anaerobic respiration.
CC Probably phosphorylates ResD. {ECO:0000269|PubMed:8631715}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBUNIT: Oligomerizes, probably forms homodimers. Interacts in vivo
CC with FloT, colocalizes with FloT-only membrane rafts. Oligomerization
CC is assisted by FloT (PubMed:26297017, PubMed:25909364). Another study
CC shows only minor colocalization with FloT membrane assemblies
CC (PubMed:27362352). {ECO:0000269|PubMed:25909364,
CC ECO:0000269|PubMed:26297017, ECO:0000269|PubMed:27362352}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:25909364};
CC Multi-pass membrane protein {ECO:0000305}. Membrane raft
CC {ECO:0000269|PubMed:25909364, ECO:0000269|PubMed:27362352}; Multi-pass
CC membrane protein {ECO:0000255}.
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DR EMBL; L09228; AAA67498.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14243.1; -; Genomic_DNA.
DR PIR; H69691; H69691.
DR RefSeq; NP_390192.1; NC_000964.3.
DR RefSeq; WP_003230520.1; NZ_JNCM01000036.1.
DR PDB; 4ZR7; X-ray; 1.86 A; A/B/C/D=40-162.
DR PDBsum; 4ZR7; -.
DR AlphaFoldDB; P35164; -.
DR SMR; P35164; -.
DR STRING; 224308.BSU23110; -.
DR PaxDb; P35164; -.
DR PRIDE; P35164; -.
DR DNASU; 938965; -.
DR EnsemblBacteria; CAB14243; CAB14243; BSU_23110.
DR GeneID; 938965; -.
DR KEGG; bsu:BSU23110; -.
DR PATRIC; fig|224308.179.peg.2518; -.
DR eggNOG; COG5002; Bacteria.
DR InParanoid; P35164; -.
DR OMA; FNQMGRQ; -.
DR PhylomeDB; P35164; -.
DR BioCyc; BSUB:BSU23110-MON; -.
DR BRENDA; 2.7.13.3; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IBA:GO_Central.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR GO; GO:0007234; P:osmosensory signaling via phosphorelay pathway; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
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; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR041328; HisK_sensor.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF18698; HisK_sensor; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..589
FT /note="Sensor histidine kinase ResE"
FT /id="PRO_0000074861"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 194..246
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 253..320
FT /note="PAS"
FT DOMAIN 371..589
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 374
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT HELIX 42..59
FT /evidence="ECO:0007829|PDB:4ZR7"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:4ZR7"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:4ZR7"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4ZR7"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:4ZR7"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:4ZR7"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:4ZR7"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:4ZR7"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:4ZR7"
SQ SEQUENCE 589 AA; 66771 MW; DD200E985E0973EE CRC64;
MKFWKSVVGK LWFTILSLVL IVLFILTVLL LEFIENYHVE EAENDLTQLA NKVAVILENH
EDQALARSIT WELADNLTSI AIIQDEKNHW YSPNDKNRLS SITVEQIQHD KDLNKALKDH
KKVSKRTGLS DTDTDNERLI VGVPYEKDGK KGMVFLSQSL LAVKDTTKHT TRYIFLAAGI
AIVLTTFFAF FLSSRVTYPL RKMREGAQDL AKGKFDTKIP ILTQDEIGEL ATAFNQMGRQ
LNFHINALNQ EKEQLSNILS SMADGVITIN IDGTILVTNP PAERFLQAWY YEQNMNIKEG
DNLPPEAKEL FQNAVSTEKE QMIEMTLQGR SWVLLMSPLY AESHVRGAVA VLRDMTEERR
LDKLREDFIA NVSHELRTPI SMLQGYSEAI VDDIASSEED RKEIAQIIYD ESLRMGRLVN
DLLDLARMES GHTGLHYEKI NVNEFLEKII RKFSGVAKEK NIALDHDISL TEEEFMFDED
KMEQVFTNLI DNALRHTSAG GSVSISVHSV KDGLKIDIKD SGSGIPEEDL PFIFERFYKA
DKARTRGRAG TGLGLAIVKN IVEAHNGSIT VHSRIDKGTT FSFYIPTKR
