ID   Q2K765_RHIEC            Unreviewed;       540 AA.
AC   Q2K765;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ABC91321.1};
GN   Name=mcpV3 {ECO:0000313|EMBL:ABC91321.1};
GN   OrderedLocusNames=RHE_CH02547 {ECO:0000313|EMBL:ABC91321.1};
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834 {ECO:0000313|EMBL:ABC91321.1, ECO:0000313|Proteomes:UP000001936};
RN   [1] {ECO:0000313|EMBL:ABC91321.1, ECO:0000313|Proteomes:UP000001936}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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; CP000133; ABC91321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2K765; -.
DR   KEGG; ret:RHE_CH02547; -.
DR   eggNOG; COG0840; Bacteria.
DR   eggNOG; COG4564; Bacteria.
DR   HOGENOM; CLU_000445_107_21_5; -.
DR   Proteomes; UP000001936; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR43531:SF11; METHYL-ACCEPTING CHEMOTAXIS PROTEIN 3; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM01049; Cache_2; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 2.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001936};
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        121..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          144..197
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          225..276
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          281..510
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   DOMAIN          440..502
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          198..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          300..344
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        198..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   540 AA;  58086 MW;  AFE0043E82BED1E6 CRC64;
     MTREQAQAAA KDVIGAMRYG ADGYFWINDM RPAMVMHPIK PQLNGTDISQ MKDPTGKFLF
     VEFVNKVKKD GKGFVDYYWP KPGADEPVLK YSYVAGFEPW GWIVGTGVYA DDLAALYRQN
     AIWAAALCLL GSAATIAIAY AIVRSVTAPI ARLKTAMNAI AAEEVSVEIA GADRRDEIGQ
     MAKALLVLRD SVDERSALRG REDERQRQIE NERRGNEASL RSASERQSRA MQALGIGLEK
     LASGDLTVSI GDIGEDYAKL RSDFNAAVDA LNGVIHAIAE SSRVVNDSAS DISEATGNLS
     KRTEQQAAAL EETAAALDEI TATVKTASER ANEAREMVAE TKASAGRSGD IVRNAVTAMG
     RIEESSSRIN QIISVIDEIA FQTNLLALNA GVEAARAGEA GRGFAVVAQE VRELAQRSAN
     AAKEIKELIS RSAAEVEGGV ALVRSTGDAL LEIEALVNQV NDHVASIATA AREQSTGLNE
     INSSVNHMDQ MTQQNAAMVE ETTAASRTLA DESTQLKSLL SNFRLREAGR QAETRYTRAA
//