MCP4_ECOLI
ID MCP4_ECOLI Reviewed; 533 AA.
AC P07018; P76300;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Methyl-accepting chemotaxis protein IV;
DE Short=MCP-IV;
DE AltName: Full=Dipeptide chemoreceptor protein;
GN Name=tap; OrderedLocusNames=b1885, JW1874;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6305515; DOI=10.1016/0092-8674(83)90442-7;
RA Krikos A., Mutoh N., Boyd A., Simon M.I.;
RT "Sensory transducers of E. coli are composed of discrete structural and
RT functional domains.";
RL Cell 33:615-622(1983).
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 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).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=22380631; DOI=10.1111/j.1365-2958.2012.08021.x;
RA Li G., Young K.D.;
RT "Isolation and identification of new inner membrane-associated proteins
RT that localize to cell poles in Escherichia coli.";
RL Mol. Microbiol. 84:276-295(2012).
CC -!- FUNCTION: Mediates taxis toward dipeptides via an interaction with the
CC periplasmic dipeptide-binding protein.
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. Attractants increase the level of methylation while
CC repellents decrease the level of methylation, the methyl groups are
CC added by the methyltransferase CheR and removed by the methylesterase
CC CheB.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22380631}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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; J01705; AAA23567.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74955.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15701.1; -; Genomic_DNA.
DR PIR; E64951; QRECM2.
DR RefSeq; NP_416399.1; NC_000913.3.
DR RefSeq; WP_000483239.1; NZ_LN832404.1.
DR AlphaFoldDB; P07018; -.
DR SMR; P07018; -.
DR BioGRID; 4262072; 172.
DR DIP; DIP-10955N; -.
DR IntAct; P07018; 2.
DR STRING; 511145.b1885; -.
DR PaxDb; P07018; -.
DR PRIDE; P07018; -.
DR EnsemblBacteria; AAC74955; AAC74955; b1885.
DR EnsemblBacteria; BAA15701; BAA15701; BAA15701.
DR GeneID; 946397; -.
DR KEGG; ecj:JW1874; -.
DR KEGG; eco:b1885; -.
DR PATRIC; fig|1411691.4.peg.362; -.
DR EchoBASE; EB0980; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR InParanoid; P07018; -.
DR OMA; QATWLEN; -.
DR PhylomeDB; P07018; -.
DR BioCyc; EcoCyc:TAP-MON; -.
DR PRO; PR:P07018; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IMP:EcoCyc.
DR GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd00181; Tar_Tsr_LBD; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR004091; Chemotax_Me-accpt_rcpt_Me-site.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SMART; SM00319; TarH; 1.
DR SUPFAM; SSF47170; SSF47170; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Chemotaxis; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..533
FT /note="Methyl-accepting chemotaxis protein IV"
FT /id="PRO_0000110541"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..188
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 269..498
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT MOD_RES 293
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250|UniProtKB:P07017"
FT MOD_RES 300
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250|UniProtKB:P05704"
FT MOD_RES 307
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250|UniProtKB:P05704"
FT MOD_RES 489
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000250|UniProtKB:P05704"
FT CONFLICT 335
FT /note="A -> G (in Ref. 1; AAA23567)"
FT /evidence="ECO:0000305"
FT CONFLICT 503
FT /note="H -> R (in Ref. 1; AAA23567)"
FT /evidence="ECO:0000305"
FT CONFLICT 527..533
FT /note="QIAPVVS -> TNCASGILK (in Ref. 1; AAA23567)"
FT /evidence="ECO:0000305"
SQ 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