ID L0M1E4_ENTBF Unreviewed; 547 AA.
AC L0M1E4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGB77744.1};
GN OrderedLocusNames=D782_1748 {ECO:0000313|EMBL:AGB77744.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB77744.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB77744.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB77744.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP003938; AGB77744.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M1E4; -.
DR STRING; 693444.D782_1748; -.
DR KEGG; ebf:D782_1748; -.
DR PATRIC; fig|693444.3.peg.1683; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_16_6; -.
DR OrthoDB; 9765776at2; -.
DR Proteomes; UP000011002; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR CDD; cd19407; Tar_Tsr_sensor; 1.
DR Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 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 PANTHER; PTHR43531:SF5; METHYL-ACCEPTING CHEMOTAXIS PROTEIN II; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
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; Aspartate receptor, ligand-binding domain; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Reference proteome {ECO:0000313|Proteomes:UP000011002};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 271..500
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 547 AA; 58895 MW; 73D7728B1B04F42B CRC64;
MLNRIRVVTL LMLVLVVFAL LQLFSGGLLF SSLSQNQHSF ALSNALRTQQ TELTDAWDLM
LQTRINLSRS SARMMMDTSN LQSSAKTDLL KNAKSTLAQA QVHITRFNQA AVEPEMAQVS
QRVAQQTQAY FAALQELIGF LEQGNMDAYF AQPTQGKQNA MGEAMGVYRA QSESLYQQAF
TTSSHDYQFA RWQLMILALV LAAVLLAVWF GIRRILLTPL NHVMTHIRHI ANGDLTPALS
LKGRNELTQL ADTVNHMQHA LIDTVTRVRE GTDAIYSGTS EIAAGNNDLS SRTEQQSASL
EETAASMEQL TATVKQNADN ARQASRLAQS ASQTARRGGD VVDNVVSTMH DIAGSSQKIA
DITSVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAGE VRNLASRSAQ AAKEIKALID
NSVERVDAGS RLVESAGETM HEIVSAVTRV TDIMGEISSA SDEQSRGIDQ VALAVTEMDK
VTQQNAALVE ESAAAAAALE EQAGKLSEAV SAFRLASSAR AVASLKTASA PVVKPAVARS
EENWETF
//