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Methyl-accepting chemotaxis protein IV (MCP-IV) (Dipeptide chemoreceptor protein)

 MCP4_ECOLI              Reviewed;         533 AA.
P07018; P76300;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
20-JUN-2018, entry version 157.
RecName: Full=Methyl-accepting chemotaxis protein IV;
Short=MCP-IV;
AltName: Full=Dipeptide chemoreceptor protein;
Name=tap; OrderedLocusNames=b1885, JW1874;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6305515; DOI=10.1016/0092-8674(83)90442-7;
Krikos A., Mutoh N., Boyd A., Simon M.I.;
"Sensory transducers of E. coli are composed of discrete structural
and functional domains.";
Cell 33:615-622(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097040; DOI=10.1093/dnares/3.6.379;
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
Yamamoto Y., Horiuchi T.;
"A 460-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 40.1-50.0 min region on the linkage map.";
DNA Res. 3:379-392(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[6]
SUBCELLULAR LOCATION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
Li G., Young K.D.;
"Isolation and identification of new inner membrane-associated
proteins that localize to cell poles in Escherichia coli.";
Mol. Microbiol. 84:276-295(2012).
-!- FUNCTION: Mediates taxis toward dipeptides via an interaction with
the periplasmic dipeptide-binding protein.
-!- FUNCTION: Chemotactic-signal transducers respond to changes in the
concentration of attractants and repellents in the environment,
transduce a signal from the outside to the inside of the cell, and
facilitate sensory adaptation through the variation of the level
of methylation. Attractants increase the level of methylation
while repellents decrease the level of methylation, the methyl
groups are added by the methyltransferase CheR and removed by the
methylesterase CheB.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:22380631}; Multi-pass membrane protein
{ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell
poles.
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EMBL; J01705; AAA23567.1; -; Genomic_DNA.
EMBL; U00096; AAC74955.1; -; Genomic_DNA.
EMBL; AP009048; BAA15701.1; -; Genomic_DNA.
PIR; E64951; QRECM2.
RefSeq; NP_416399.1; NC_000913.3.
RefSeq; WP_000483239.1; NZ_LN832404.1.
ProteinModelPortal; P07018; -.
SMR; P07018; -.
BioGrid; 4262072; 172.
DIP; DIP-10955N; -.
IntAct; P07018; 2.
STRING; 316385.ECDH10B_2026; -.
PaxDb; P07018; -.
PRIDE; P07018; -.
EnsemblBacteria; AAC74955; AAC74955; b1885.
EnsemblBacteria; BAA15701; BAA15701; BAA15701.
GeneID; 946397; -.
KEGG; ecj:JW1874; -.
KEGG; eco:b1885; -.
PATRIC; fig|1411691.4.peg.362; -.
EchoBASE; EB0980; -.
EcoGene; EG10987; tap.
eggNOG; ENOG4105C8Q; Bacteria.
eggNOG; COG0840; LUCA.
HOGENOM; HOG000148074; -.
InParanoid; P07018; -.
KO; K05877; -.
OMA; QATWLEN; -.
PhylomeDB; P07018; -.
BioCyc; EcoCyc:TAP-MONOMER; -.
PRO; PR:P07018; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:EcoCyc.
GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
CDD; cd06225; HAMP; 1.
CDD; cd00181; Tar_Tsr_LBD; 1.
InterPro; IPR035440; 4HB_MCP_dom_sf.
InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
InterPro; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
InterPro; IPR003660; HAMP_dom.
InterPro; IPR004089; MCPsignal_dom.
InterPro; IPR003122; Tar_rcpt_lig-bd.
Pfam; PF00672; HAMP; 1.
Pfam; PF00015; MCPsignal; 1.
Pfam; PF02203; TarH; 1.
PRINTS; PR00260; CHEMTRNSDUCR.
SMART; SM00304; HAMP; 1.
SMART; SM00283; MA; 1.
SMART; SM00319; TarH; 1.
SUPFAM; SSF47170; SSF47170; 1.
PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PROSITE; PS50885; HAMP; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Chemotaxis; Complete proteome;
Membrane; Methylation; Reference proteome; Transducer; Transmembrane;
Transmembrane helix.
CHAIN 1 533 Methyl-accepting chemotaxis protein IV.
/FTId=PRO_0000110541.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 33 Helical. {ECO:0000255}.
TOPO_DOM 34 188 Periplasmic. {ECO:0000255}.
TRANSMEM 189 209 Helical. {ECO:0000255}.
TOPO_DOM 210 533 Cytoplasmic. {ECO:0000255}.
DOMAIN 212 264 HAMP. {ECO:0000255|PROSITE-
ProRule:PRU00102}.
DOMAIN 269 498 Methyl-accepting transducer.
{ECO:0000255|PROSITE-ProRule:PRU00284}.
MOD_RES 293 293 Glutamate methyl ester (Gln).
{ECO:0000250|UniProtKB:P07017}.
MOD_RES 300 300 Glutamate methyl ester (Gln).
{ECO:0000250|UniProtKB:P05704}.
MOD_RES 307 307 Glutamate methyl ester (Gln).
{ECO:0000250|UniProtKB:P05704}.
MOD_RES 489 489 Glutamate methyl ester (Glu).
{ECO:0000250|UniProtKB:P05704}.
CONFLICT 335 335 A -> G (in Ref. 1; AAA23567).
{ECO:0000305}.
CONFLICT 503 503 H -> R (in Ref. 1; AAA23567).
{ECO:0000305}.
CONFLICT 527 533 QIAPVVS -> TNCASGILK (in Ref. 1;
AAA23567). {ECO:0000305}.
SEQUENCE 533 AA; 57512 MW; 632570BE1E45DA38 CRC64;
MFNRIRISTT LFLILILCGI LQIGSNGMSF WAFRDDLQRL NQVEQSNQQR AALAQTRAVM
LQASTALNKA GTLTALSYPA DDIKTLMTTA RASLTQSTTL FKSFMAMTAG NEHVRGLQKE
TEKSFARWHN DLEHQATWLE SNQLSDFLTA PVQGSQNAFD VNFEAWQLEI NHVLEAASAQ
SQRNYQISAL VFISMIIVAA IYISSALWWT RKMIVQPLAI IGSHFDSIAA GNLARPIAVY
GRNEITAIFA SLKTMQQALR GTVSDVRKGS QEMHIGIAEI VAGNNDLSSR TEQQAASLAQ
TAASMEQLTA TVGQNADNAR QASELAKNAA TTAQAGGVQV STMTHTMQEI ATSSQKIGDI
ISVIDGIAFQ TNILALNAAV EAARAGEQGR GFAVVAGEVR NLASRSAQAA KEIKGLIEES
VNRVQQGSKL VNNAAATMID IVSSVTRVND IMGEIASASE EQQRGIEQVA QAVSQMDQVT
QQNASLVEEA AVATEQLANQ ADHLSSRVAV FTLEEHEVAR HESVQLQIAP VVS


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