MCP10_MAGSA
ID MCP10_MAGSA Reviewed; 436 AA.
AC Q2W8M7;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Methyl-accepting chemotaxis protein Amb0994 {ECO:0000303|PubMed:20471399};
DE AltName: Full=Putative torque-sensing protein Amb0994 {ECO:0000305};
GN OrderedLocusNames=amb0994;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
RN [2]
RP FUNCTION, INTERACTION WITH MAMK, SUBCELLULAR LOCATION, DOMAIN, AND POSSIBLE
RP METHYLATION AT GLU-225.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=20471399; DOI=10.1016/j.jmb.2010.05.011;
RA Philippe N., Wu L.F.;
RT "An MCP-like protein interacts with the MamK cytoskeleton and is involved
RT in magnetotaxis in Magnetospirillum magneticum AMB-1.";
RL J. Mol. Biol. 400:309-322(2010).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=24877161; DOI=10.1039/c3ib40259b;
RA Zhu X., Ge X., Li N., Wu L.F., Luo C., Ouyang Q., Tu Y., Chen G.;
RT "Angle sensing in magnetotaxis of Magnetospirillum magneticum AMB-1.";
RL Integr. Biol. (Camb.) 6:706-713(2014).
CC -!- FUNCTION: Probable methyl-accepting taxis protein. May be the receptor
CC that senses the torque generated from the interaction between the
CC magnetosome dipole moment and the external magnetic field (Probable).
CC Overproduction interferes with magnetotaxis, cells respond more slowly
CC to changes in the magnetic field; requires the MamK-interacting C-
CC terminus of the protein. The effect of magnetic sensing is to control
CC flagellar rotation (PubMed:20471399). {ECO:0000269|PubMed:20471399,
CC ECO:0000305|PubMed:24877161}.
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 variation of methylation levels.
CC Attractants increase the level of methylation while repellents decrease
CC the level of methylation. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with MamK at cell poles and septa.
CC {ECO:0000269|PubMed:20471399}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:20471399}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Found predominantly at cell poles or at septa where
CC divison occurs. {ECO:0000269|PubMed:20471399}.
CC -!- DOMAIN: Only the C-terminus (residues 321-436) is necessary to interact
CC with MamK; its addition to MCP25 confers the ability to interact with
CC MamK. {ECO:0000269|PubMed:20471399}.
CC -!- DISRUPTION PHENOTYPE: A double amb0994-amb0995 deletion grows normally
CC and has wild-type magnetosomes. It fails to sense and respond to an
CC external magnetic field, i.e. bacteria do not align to the field.
CC {ECO:0000269|PubMed:24877161}.
CC -!- MISCELLANEOUS: This bacteria makes up to 20 cubo-octahedral
CC magnetosomes of about 45 nm in diameter which contain membrane-bound
CC crystals of magnetite (Fe(3)O(4)). {ECO:0000305}.
CC -!- MISCELLANEOUS: There are over 60 methyl-accepting chemotaxis proteins
CC in this bacterium. {ECO:0000269|PubMed:16303747}.
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; AP007255; BAE49798.1; -; Genomic_DNA.
DR RefSeq; WP_011383420.1; NC_007626.1.
DR AlphaFoldDB; Q2W8M7; -.
DR SMR; Q2W8M7; -.
DR STRING; 342108.amb0994; -.
DR EnsemblBacteria; BAE49798; BAE49798; amb0994.
DR KEGG; mag:amb0994; -.
DR HOGENOM; CLU_000445_107_27_5; -.
DR OMA; MRTATHE; -.
DR OrthoDB; 429006at2; -.
DR Proteomes; UP000007058; Chromosome.
DR GO; GO:0060187; C:cell pole; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0110148; P:biomineralization; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Cell inner membrane; Cell membrane; Membrane;
KW Methylation; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..436
FT /note="Methyl-accepting chemotaxis protein Amb0994"
FT /id="PRO_0000447748"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 180..416
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT REGION 321..436
FT /note="Required for interaction with MamK and to respond to
FT the magnetic field"
FT /evidence="ECO:0000269|PubMed:20471399"
FT MOD_RES 211
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000250|UniProtKB:P02942"
FT MOD_RES 225
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000305|PubMed:20471399"
SQ SEQUENCE 436 AA; 44582 MW; B21FB822E866E491 CRC64;
METTLGSYAR TLSLGMLVPS AICLLAGTFG LLGGSSIALW VVIAVSLLGV VGGVKIGGSA
RRMAGDLSTA IHVLSRSASG DLNARILDVR GSGGIGALQH SINRLLDLAE AFGKEAFAAV
ESANHGRYYR RIITTGLRGD FVLYAKTINQ ALKRMEARDA EFIAFANNQV KPVVNAVAAA
ATELEASSGA MSAQSTDTSH QAMTVAAAAE QASVNVQAVA SAVEEFSASI KEISTQVHRA
AAVASEAAGV ASRTDTTVHG LSDAAQRIGA IVSLINDIAA QTNLLALNAT IEAARAGDAG
KGFAVVANEV KNLANQTARA TEDITSQVAH IQEVAAEAIK AIQEITRTVS QIEETSSAVA
GAVEEQNAVT VEIARNVAEA ATGTSSVSSA IITVQATAAE ATESAGQVAD AASELSRQSE
NLSREVDGFI ARIGGR
