ZRAS_ECOLI
ID ZRAS_ECOLI Reviewed; 465 AA.
AC P14377; Q2M8U0;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Sensor protein ZraS;
DE EC=2.7.13.3;
GN Name=zraS; Synonyms=hydH; OrderedLocusNames=b4003, JW3967;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-465.
RC STRAIN=K12;
RX PubMed=2666400; DOI=10.1128/jb.171.8.4448-4456.1989;
RA Stoker K., Reijnders W.N.M., Oltmann L.F., Stouthamer A.H.;
RT "Initial cloning and sequencing of hydHG, an operon homologous to ntrBC and
RT regulating the labile hydrogenase activity in Escherichia coli K-12.";
RL J. Bacteriol. 171:4448-4456(1989).
RN [5]
RP CHARACTERIZATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11243806; DOI=10.1006/jmbi.2000.4451;
RA Leonhartsberger S., Huber A., Lottspeich F., Boeck A.;
RT "The hydH/G genes from Escherichia coli code for a zinc and lead responsive
RT two-component regulatory system.";
RL J. Mol. Biol. 307:93-105(2001).
RN [6]
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 [7]
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).
CC -!- FUNCTION: Member of the two-component regulatory system ZraS/ZraR. May
CC function as a membrane-associated protein kinase that phosphorylates
CC ZraR in response to high concentrations of zinc or lead in the medium.
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
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- PTM: Autophosphorylated.
CC -!- CAUTION: Was originally thought to be involved in the regulation of the
CC labile hydrogenase activity. {ECO:0000305|PubMed:2666400}.
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DR EMBL; U00006; AAC43101.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76977.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77316.1; -; Genomic_DNA.
DR EMBL; M28369; AAA24003.1; -; Genomic_DNA.
DR PIR; F65207; F65207.
DR RefSeq; NP_418431.1; NC_000913.3.
DR RefSeq; WP_001211892.1; NZ_SSZK01000047.1.
DR AlphaFoldDB; P14377; -.
DR SMR; P14377; -.
DR BioGRID; 4263453; 21.
DR DIP; DIP-9981N; -.
DR IntAct; P14377; 1.
DR STRING; 511145.b4003; -.
DR PaxDb; P14377; -.
DR PRIDE; P14377; -.
DR EnsemblBacteria; AAC76977; AAC76977; b4003.
DR EnsemblBacteria; BAE77316; BAE77316; BAE77316.
DR GeneID; 948506; -.
DR KEGG; ecj:JW3967; -.
DR KEGG; eco:b4003; -.
DR PATRIC; fig|1411691.4.peg.2707; -.
DR EchoBASE; EB0008; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_89_29_6; -.
DR InParanoid; P14377; -.
DR OMA; QAIFTPY; -.
DR PhylomeDB; P14377; -.
DR BioCyc; EcoCyc:HYDH-MON; -.
DR BioCyc; MetaCyc:HYDH-MON; -.
DR BRENDA; 2.7.13.3; 2026.
DR PRO; PR:P14377; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
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; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IDA:EcoCyc.
DR GO; GO:0036460; P:cellular response to cell envelope stress; IEP:EcoCyc.
DR GO; GO:0071284; P:cellular response to lead ion; IEP:EcoCyc.
DR GO; GO:0071294; P:cellular response to zinc ion; IEP:EcoCyc.
DR GO; GO:0018106; P:peptidyl-histidine phosphorylation; ISM: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; 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; IPR029151; Sensor-like_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; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF103190; SSF103190; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 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; Zinc.
FT CHAIN 1..465
FT /note="Sensor protein ZraS"
FT /id="PRO_0000074909"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 251..458
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 254
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 361
FT /note="L -> V (in Ref. 4; AAA24003)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..387
FT /note="SESGA -> TKAG (in Ref. 4; AAA24003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 51032 MW; 0472AC3494E95EE3 CRC64;
MRFMQRSKDS LAKWLSAILP VVIVGLVGLF AVTVIRDYGR ASEADRQALL EKGNVLIRAL
ESGSRVGMGM RMHHVQQQAL LEEMAGQPGV LWFAVTDAQG IIILHSDPDK VGRALYSPDE
MQKLKPEENS RWRLLGKTET TPALEVYRLF QPMSAPWRHG MHNMPRCNGK AVPQVDAQQA
IFIAVDASDL VATQSGEKRN TLIILFALAT VLLASVLSFF WYRRYLRSRQ LLQDEMKRKE
KLVALGHLAA GVAHEIRNPL SSIKGLAKYF AERAPAGGEA HQLAQVMAKE ADRLNRVVSE
LLELVKPTHL ALQAVDLNTL INHSLQLVSQ DANSREIQLR FTANDTLPEI QADPDRLTQV
LLNLYLNAIQ AIGQHGVISV TASESGAGVK ISVTDSGKGI AADQLDAIFT PYFTTKAEGT
GLGLAVVHNI VEQHGGTIQV ASQEGKGSTF TLWLPVNITR KDPQG
