BAES_ECOLI
ID BAES_ECOLI Reviewed; 467 AA.
AC P30847; P76401;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Signal transduction histidine-protein kinase BaeS;
DE EC=2.7.13.3;
GN Name=baeS {ECO:0000303|PubMed:8282725}; OrderedLocusNames=b2078, JW2063;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8282725; DOI=10.1093/oxfordjournals.jbchem.a124180;
RA Nagasawa S., Ishige K., Mizuno T.;
RT "Novel members of the two-component signal transduction genes in
RT Escherichia coli.";
RL J. Biochem. 114:350-357(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN REGULATION OF THE MDTABCD OPERON.
RC STRAIN=K12;
RX PubMed=12107134; DOI=10.1128/jb.184.15.4168-4176.2002;
RA Baranova N., Nikaido H.;
RT "The baeSR two-component regulatory system activates transcription of the
RT yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and
RT increases its resistance to novobiocin and deoxycholate.";
RL J. Bacteriol. 184:4168-4176(2002).
RN [6]
RP FUNCTION IN ENVELOPE STRESS RESPONSE.
RC STRAIN=K12 / MC4100;
RX PubMed=12354228; DOI=10.1046/j.1365-2958.2002.03112.x;
RA Raffa R.G., Raivio T.L.;
RT "A third envelope stress signal transduction pathway in Escherichia coli.";
RL Mol. Microbiol. 45:1599-1611(2002).
RN [7]
RP FUNCTION, AND AUTOPHOSPHORYLATION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=15522865; DOI=10.1074/jbc.m410104200;
RA Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., Ishihama A.;
RT "Functional characterization in vitro of all two-component signal
RT transduction systems from Escherichia coli.";
RL J. Biol. Chem. 280:1448-1456(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP REGULATION OF THE CASABCDE-YGBT-YGBF OPERON, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=21255106; DOI=10.1111/j.1365-2958.2010.07482.x;
RA Perez-Rodriguez R., Haitjema C., Huang Q., Nam K.H., Bernardis S., Ke A.,
RA DeLisa M.P.;
RT "Envelope stress is a trigger of CRISPR RNA-mediated DNA silencing in
RT Escherichia coli.";
RL Mol. Microbiol. 79:584-599(2011).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ARG-150; PRO-192; GLU-264; ASP-268 AND
RP ARG-416.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21317898; DOI=10.1038/nsmb.2016;
RA Quan S., Koldewey P., Tapley T., Kirsch N., Ruane K.M., Pfizenmaier J.,
RA Shi R., Hofmann S., Foit L., Ren G., Jakob U., Xu Z., Cygler M.,
RA Bardwell J.C.;
RT "Genetic selection designed to stabilize proteins uncovers a chaperone
RT called Spy.";
RL Nat. Struct. Mol. Biol. 18:262-269(2011).
CC -!- FUNCTION: Member of the two-component regulatory system BaeS/BaeR which
CC responds to envelope stress (PubMed:12354228, PubMed:21317898).
CC Activates expression of periplasmic chaperone spy in response to
CC spheroplast formation, indole and P pili protein PapG overexpression
CC (PubMed:12354228). Activates BaeR by phosphorylation which then
CC activates the mdtABCD (PubMed:12107134) and probably the CRISPR-Cas
CC casABCDE-ygbT-ygbF operons (PubMed:21255106).
CC {ECO:0000269|PubMed:12354228, ECO:0000269|PubMed:15522865,
CC ECO:0000269|PubMed:21255106, ECO:0000269|PubMed:21317898}.
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 inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:15522865}.
CC -!- DISRUPTION PHENOTYPE: Loss of induction of the CRISPR-Cas casABCDE-
CC ygbT-ygbF operon (PubMed:21255106). {ECO:0000269|PubMed:21255106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D14054; BAA03140.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75139.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15934.1; -; Genomic_DNA.
DR PIR; E64974; E64974.
DR RefSeq; NP_416582.1; NC_000913.3.
DR RefSeq; WP_000675150.1; NZ_SSZK01000011.1.
DR AlphaFoldDB; P30847; -.
DR SMR; P30847; -.
DR BioGRID; 4260426; 47.
DR DIP; DIP-9199N; -.
DR IntAct; P30847; 3.
DR STRING; 511145.b2078; -.
DR jPOST; P30847; -.
DR PaxDb; P30847; -.
DR PRIDE; P30847; -.
DR EnsemblBacteria; AAC75139; AAC75139; b2078.
DR EnsemblBacteria; BAA15934; BAA15934; BAA15934.
DR GeneID; 66674022; -.
DR GeneID; 946611; -.
DR KEGG; ecj:JW2063; -.
DR KEGG; eco:b2078; -.
DR PATRIC; fig|1411691.4.peg.172; -.
DR EchoBASE; EB1574; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_89_6_6; -.
DR InParanoid; P30847; -.
DR OMA; RTSWLIV; -.
DR PhylomeDB; P30847; -.
DR BioCyc; EcoCyc:BAES-MON; -.
DR BioCyc; MetaCyc:BAES-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P30847; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IDA:EcoCyc.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IDA:EcoCyc.
DR CDD; cd00082; HisKA; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response;
KW Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..467
FT /note="Signal transduction histidine-protein kinase BaeS"
FT /id="PRO_0000074696"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..167
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..467
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 187..239
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 247..461
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 250
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MUTAGEN 150
FT /note="R->W: Increased expression of periplasmic chaperone
FT Spy."
FT /evidence="ECO:0000269|PubMed:21317898"
FT MUTAGEN 192
FT /note="P->L: Increased expression of periplasmic chaperone
FT Spy."
FT /evidence="ECO:0000269|PubMed:21317898"
FT MUTAGEN 264
FT /note="E->K: Increased expression of periplasmic chaperone
FT Spy."
FT /evidence="ECO:0000269|PubMed:21317898"
FT MUTAGEN 268
FT /note="D->N: Increased expression of periplasmic chaperone
FT Spy."
FT /evidence="ECO:0000269|PubMed:21317898"
FT MUTAGEN 416
FT /note="R->C: Increased expression of periplasmic chaperone
FT Spy, increased mRNA for mdtA and acrD, target genes of the
FT BaeSR envelope stress response."
FT /evidence="ECO:0000269|PubMed:21317898"
FT CONFLICT 414..421
FT /note="GSRNRASG -> VPATVPA (in Ref. 1; BAA03140)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 51991 MW; 024D76950012FFE0 CRC64;
MKFWRPGITG KLFLAIFATC IVLLISMHWA VRISFERGFI DYIKHGNEQR LQLLSDALGE
QYAQHGNWRF LRNNDRFVFQ ILRSFEHDNS EDKPGPGMPP HGWRTQFWVV DQNNKVLVGP
RAPIPPDGTR RPILVNGAEV GAVIASPVER LTRNTDINFD KQQRQTSWLI VALATLLAAL
ATFLLARGLL APVKRLVDGT HKLAAGDFTT RVTPTSEDEL GKLAQDFNQL ASTLEKNQQM
RRDFMADISH ELRTPLAVLR GELEAIQDGV RKFTPETVAS LQAEVGTLTK LVDDLHQLSM
SDEGALAYQK APVDLIPLLE VAGGAFRERF ASRGLKLQFS LPDSITVFGD RDRLMQLFNN
LLENSLRYTD SGGSLQISAG QRDKTVRLTF ADSAPGVSDD QLQKLFERFY RTEGSRNRAS
GGSGLGLAIC LNIVEAHNGR IIAAHSPFGG VSITVELPLE RDLQREV
