BASS_ECOLI
ID BASS_ECOLI Reviewed; 363 AA.
AC P30844; Q2M6J2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Sensor protein BasS;
DE EC=2.7.13.3;
GN Name=basS; Synonyms=pmrB; OrderedLocusNames=b4112, JW4073;
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 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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, 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 [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
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).
CC -!- FUNCTION: Member of the two-component regulatory system BasS/BasR
CC Autophosphorylates and activates BasR by phosphorylation.
CC {ECO:0000269|PubMed:15522865}.
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; Multi-pass membrane protein.
CC -!- INDUCTION: The eptA-basRS operon is positively autoregulated by BasR
CC under high iron or aluminum concentration conditions. {ECO:0000250}.
CC -!- PTM: Autophosphorylated.
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DR EMBL; D14055; BAA03144.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97011.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77073.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78114.1; -; Genomic_DNA.
DR PIR; JX0285; JX0285.
DR RefSeq; NP_418536.1; NC_000913.3.
DR RefSeq; WP_001300761.1; NZ_CP047127.1.
DR AlphaFoldDB; P30844; -.
DR SMR; P30844; -.
DR BioGRID; 4263084; 4.
DR DIP; DIP-9202N; -.
DR IntAct; P30844; 4.
DR STRING; 511145.b4112; -.
DR jPOST; P30844; -.
DR PaxDb; P30844; -.
DR PRIDE; P30844; -.
DR EnsemblBacteria; AAC77073; AAC77073; b4112.
DR EnsemblBacteria; BAE78114; BAE78114; BAE78114.
DR GeneID; 948632; -.
DR KEGG; ecj:JW4073; -.
DR KEGG; eco:b4112; -.
DR PATRIC; fig|83333.103.peg.419; -.
DR EchoBASE; EB1571; -.
DR eggNOG; COG0642; Bacteria.
DR HOGENOM; CLU_000445_89_37_6; -.
DR InParanoid; P30844; -.
DR OMA; QLISVFW; -.
DR PhylomeDB; P30844; -.
DR BioCyc; EcoCyc:BASS-MON; -.
DR BioCyc; MetaCyc:BASS-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P30844; -.
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:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:EcoCyc.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:EcoCyc.
DR GO; GO:0010041; P:response to iron(III) ion; IDA:EcoCyc.
DR GO; GO:0010043; P:response to zinc ion; IEP: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; 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; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..363
FT /note="Sensor protein BasS"
FT /id="PRO_0000074701"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..64
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 89..141
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 149..357
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 152
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 363 AA; 41029 MW; A390AAB9EB425750 CRC64;
MHFLRRPISL RQRLILTIGA ILLVFELISV FWLWHESTEQ IQLFEQALRD NRNNDRHIMR
EIREAVASLI VPGVFMVSLT LFICYQAVRR ITRPLAELQK ELEARTADNL TPIAIHSATL
EIEAVVSALN DLVSRLTSTL DNERLFTADV AHELRTPLAG VRLHLELLAK THHIDVAPLV
ARLDQMMESV SQLLQLARAG QSFSSGNYQH VKLLEDVILP SYDELSTMLD QRQQTLLLPE
SAADITVQGD ATLLRMLLRN LVENAHRYSP QGSNIMIKLQ EDDGAVMAVE DEGPGIDESK
CGELSKAFVR MDSRYGGIGL GLSIVSRITQ LHHGQFFLQN RQETSGTRAW VRLKKDQYVA
NQI
